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		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:10858363&amp;diff=1504198</id>
		<title>PMID:10858363</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:10858363&amp;diff=1504198"/>
		<updated>2016-08-19T10:16:24Z</updated>

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&#039;&#039;&#039;Sabaté, M, Tarragó, R, Navarro, F, Miró, E, Vergés, C, Barbé, J and Prats, G&#039;&#039;&#039;  (2000) Cloning and sequence of the gene encoding a novel cefotaxime-hydrolyzing beta-lactamase (CTX-M-9) from Escherichia coli in Spain. &#039;&#039;Antimicrob. Agents Chemother.&#039;&#039; &#039;&#039;&#039;44&#039;&#039;&#039;:1970-3&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
A new CTX-M-type beta-lactamase (CTX-M-9) has been cloned from a clinical cefotaxime-resistant Escherichia coli strain. Despite the close identity that exists between the CTX-M-9 and Toho-2 beta-lactamases (88%), the 35 amino acids located between residues Ala-185 and Ala-219 are totally different in both enzymes. Outside of this region there are only six amino acids substitutions between both proteins.&lt;br /&gt;
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!align=left  |Links&lt;br /&gt;
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=10858363 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC89994 PMC89994]&lt;br /&gt;
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!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Cefotaxime/metabolism; Cefotaxime/pharmacology; Cephalosporins/metabolism; Cephalosporins/pharmacology; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Hydrolysis; Molecular Sequence Data; Sequence Homology, Amino Acid; Spain; beta-Lactamases/genetics; beta-Lactamases/metabolism&lt;br /&gt;
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		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:10858363&amp;diff=1504197</id>
		<title>PMID:10858363</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:10858363&amp;diff=1504197"/>
		<updated>2016-08-19T10:16:24Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:7994604&amp;diff=1504196</id>
		<title>PMID:7994604</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:7994604&amp;diff=1504196"/>
		<updated>2016-08-19T09:36:23Z</updated>

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{|   id=&amp;quot;L57b6d31688f7c&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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&#039;&#039;&#039;Ferat, JL, Le Gouar, M and Michel, F&#039;&#039;&#039;  (1994) Multiple group II self-splicing introns in mobile DNA from Escherichia coli. &#039;&#039;C. R. Acad. Sci. III, Sci. Vie&#039;&#039; &#039;&#039;&#039;317&#039;&#039;&#039;:141-8&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
By PCR (polymerase chain reaction) amplification and cloning, we have identified four group II self-splicing introns encoding proteins related to reverse transcriptases in natural Escherichia coli isolates belonging to the ECOR collection. One intron, IntD, interrupts a DNA sequence virtually identical to that of the previously described IS3411 Insertion Sequence. A second intron, IntC, is located within an open reading frame that is closely related to a reading frame in the T-DNA of Agrobacterium tumefaciens. Finally, introns IntA and IntB are inserted at two distinct sites in one of the Rhs elements of E. coli. A comparison of their open reading frames shows that the two Rhs introns are more closely related to each other than to any other known group II intron: this suggests that transposition of group II introns may occur preferentially in cis, along the same piece of DNA.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=7994604 PubMed]&lt;br /&gt;
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!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
DNA Transposable Elements/drug effects; DNA Transposable Elements/genetics; Escherichia coli/genetics; Introns/genetics; Molecular Sequence Data; Open Reading Frames/genetics; Phylogeny; Polymerase Chain Reaction; RNA, Catalytic/pharmacology&lt;br /&gt;
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&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:7994604&amp;diff=1504195</id>
		<title>PMID:7994604</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:7994604&amp;diff=1504195"/>
		<updated>2016-08-19T09:36:22Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:16788177&amp;diff=1504194</id>
		<title>PMID:16788177</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:16788177&amp;diff=1504194"/>
		<updated>2016-08-19T09:06:22Z</updated>

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{|   id=&amp;quot;R57b6cc0d0d416&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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&#039;&#039;&#039;Prosseda, G, Latella, MC, Casalino, M, Nicoletti, M, Michienzi, S and Colonna, B&#039;&#039;&#039;  (2006) Plasticity of the P junc promoter of ISEc11, a new insertion sequence of the IS1111 family. &#039;&#039;J. Bacteriol.&#039;&#039; &#039;&#039;&#039;188&#039;&#039;&#039;:4681-9&lt;br /&gt;
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!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
We describe identification and functional characterization of ISEc11, a new insertion sequence that is widespread in enteroinvasive E. coli (EIEC), in which it is always present on the virulence plasmid (pINV) and very frequently also present on the chromosome. ISEc11 is flanked by subterminal 13-bp inverted repeats (IRs) and is bounded by 3-bp terminal sequences, and it transposes with target specificity without generating duplication of the target site. ISEc11 is characterized by an atypical transposase containing the DEDD motif of the Piv/MooV family of DNA recombinases, and it is closely related to the IS1111 family. Transposition occurs by formation of minicircles through joining of the abutted ends and results in assembly of a junction promoter (P juncC) containing a -10 box in the interstitial sequence and a -35 box upstream of the right IR. A natural variant of ISEc11 (ISEc11p), found on EIEC pINV plasmids, contains a perfect duplication of the outermost 39 bp of the right end. Upon circularization, ISEc11p forms a junction promoter (P juncP) which, despite carrying -10 and -35 boxes identical to those of P juncC, exhibits 30-fold-greater strength in vivo. The discovery of only one starting point in primer extension experiments rules out the possibility that there are alternative promoter sites within the 39-bp duplication. Analysis of in vitro-generated transcripts confirmed that at limiting RNA polymerase concentrations, the activity of P juncP is 20-fold higher than the activity of P juncC. These observations suggest that the 39-bp duplication might host cis-acting elements that facilitate the binding of RNA polymerase to the promoter.&lt;br /&gt;
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!align=left  |Links&lt;br /&gt;
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=16788177 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1483014 PMC1483014]&lt;br /&gt;
Online version:[http://dx.doi.org/10.1128/JB.00332-06 10.1128/JB.00332-06]&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Base Sequence; Chromosomes/genetics; DNA Transposable Elements/genetics; Dysentery, Bacillary/microbiology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli/pathogenicity; Escherichia coli Infections/microbiology; Humans; Molecular Sequence Data; Plasmids/genetics; Promoter Regions, Genetic; Shigella flexneri/genetics; Shigella flexneri/metabolism; Shigella flexneri/pathogenicity; Transposases/metabolism; Virulence&lt;br /&gt;
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		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:16788177&amp;diff=1504193</id>
		<title>PMID:16788177</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:16788177&amp;diff=1504193"/>
		<updated>2016-08-19T09:06:20Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:16595675&amp;diff=1503648</id>
		<title>PMID:16595675</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:16595675&amp;diff=1503648"/>
		<updated>2016-06-15T10:19:04Z</updated>

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{|   id=&amp;quot;R57612b9785fcf&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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&#039;&#039;&#039;Xiao, J, Dai, R, Negyessy, L and Bergson, C&#039;&#039;&#039;  (2006) Calcyon, a novel partner of clathrin light chain, stimulates clathrin-mediated endocytosis. &#039;&#039;J. Biol. Chem.&#039;&#039; &#039;&#039;&#039;281&#039;&#039;&#039;:15182-93&lt;br /&gt;
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!align=left  |Abstract&lt;br /&gt;
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In the central nervous system, clathrin-mediated endocytosis is crucial for efficient synaptic transmission. Clathrin-coated vesicle assembly and disassembly is regulated by some 30 adaptor and accessory proteins, most of which interact with clathrin heavy chain. Using the calcyon cytosolic domain as bait, we isolated clathrin light chain in a yeast two-hybrid screen. The interaction domain was mapped to the heavy chain binding domain and C-terminal regions of light chain. Further, the addition of the calcyon C terminus stimulated clathrin self-assembly in a dose-dependent fashion. Calcyon, which is a single transmembrane protein predominantly expressed in brain, localized to vesicular compartments within pre- and postsynaptic structures. There was a high degree of overlap in the distribution of LC and calcyon in neuronal dendrites, spines, and cell bodies. Co-immunoprecipitation studies further suggested an association of calcyon with the clathrin-mediated endocytic machinery. Compared with controls, HEK293 cells overexpressing calcyon exhibited significantly enhanced transferrin uptake but equivalent levels of recycling. Conversely, transferrin uptake was largely abolished in neocortical neurons obtained from mice homozygous for a calcyon null allele, whereas recycling proceeded at wild type levels. Collectively, these data indicate a role for calcyon in clathrin-mediated endocytosis in brain.&lt;br /&gt;
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=16595675 PubMed]&lt;br /&gt;
Online version:[http://dx.doi.org/10.1074/jbc.M600265200 10.1074/jbc.M600265200]&lt;br /&gt;
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!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Animals; Base Sequence; Binding Sites; Cell Line; Cells, Cultured; Central Nervous System/physiology; Clathrin Light Chains/chemistry; Clathrin Light Chains/genetics; Clathrin Light Chains/metabolism; Endocytosis/physiology; Humans; In Vitro Techniques; Macaca mulatta; Membrane Proteins/chemistry; Membrane Proteins/deficiency; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mice; Mice, Knockout; Microscopy, Electron; Nerve Tissue Proteins/chemistry; Nerve Tissue Proteins/genetics; Nerve Tissue Proteins/metabolism; Neurons/metabolism; Prefrontal Cortex/metabolism; Prefrontal Cortex/ultrastructure; Protein Structure, Tertiary; Rats; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Synaptic Transmission/physiology; Two-Hybrid System Techniques&lt;br /&gt;
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		<author><name>38.100.21.109</name></author>
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		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:16595675&amp;diff=1503647</id>
		<title>PMID:16595675</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:16595675&amp;diff=1503647"/>
		<updated>2016-06-15T10:19:03Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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		<author><name>38.100.21.109</name></author>
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:7959065&amp;diff=1503640</id>
		<title>PMID:7959065</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:7959065&amp;diff=1503640"/>
		<updated>2016-05-14T04:08:01Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;K5736a4a0e0728&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Paton, AW and Paton, JC&#039;&#039;&#039;  (1994) Characterization of IS1203, an insertion sequence in Escherichia coli O111:H-. &#039;&#039;Gene&#039;&#039; &#039;&#039;&#039;150&#039;&#039;&#039;:67-70&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
The complete nucleotide (nt) sequence of IS1203 from Escherichia coli O111:H- strain PH has been determined. IS1203 is 1312-nt long, with imperfect 26-bp terminal inverted repeats. The two major ORFs in IS1203 encode polypeptides of 12.7 and 33.7 kDa, the latter being the putative transposase. IS1203 is closely related to IS629 of Shigella sonnei and IS3411 of E. coli. At least twelve copies of IS1203 were found in the genome of E. coli O111:H- strain PH.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=7959065 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Base Sequence; DNA Transposable Elements; DNA, Bacterial; Escherichia coli/genetics; Molecular Sequence Data&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:7959065&amp;diff=1503639</id>
		<title>PMID:7959065</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:7959065&amp;diff=1503639"/>
		<updated>2016-05-14T04:08:00Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2034216&amp;diff=1503638</id>
		<title>PMID:2034216</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2034216&amp;diff=1503638"/>
		<updated>2016-05-10T14:29:53Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;O5731f0612e7b9&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Iwasaki, H, Ishino, Y, Toh, H, Nakata, A and Shinagawa, H&#039;&#039;&#039;  (1991) Escherichia coli DNA polymerase II is homologous to alpha-like DNA polymerases. &#039;&#039;Mol. Gen. Genet.&#039;&#039; &#039;&#039;&#039;226&#039;&#039;&#039;:24-33&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
The Escherichia coli polB gene encodes DNA polymerase II and is regulated by the SOS system. We sequenced a 4081 nucleotide segment of the E. coli chromosome that contains the polB gene and its flanking regions. DNA polymerase II, as deduced from the DNA sequence, consists of 782 amino acids, has a molecular weight of 89,917, and is structurally homologous to alpha-like DNA polymerases, which include eukaryotic replicative DNA polymerases. Comparison of the sequences of the alpha-like DNA polymerases including E. coli DNA polymerase II showed that there were nine highly conserved regions, and we constructed an unrooted phylogenetic tree of the DNA polymerases based on the differences in these conserved regions. The DNA polymerases of herpes groups viruses and the DNA polymerases that use protein priming for the initiation of replication form two separate subfamilies that occupy opposite locations in the tree. Other DNA polymerases, including E. coli DNA polymerase II, human DNA polymerase alpha, and yeast DNA polymerase I, occupy the central regions between the two subfamilies and they are rather distantly related to each other. The transcription initiation site of polB was identified by analysis of in vivo transcripts, and the promoter was assigned upstream of the polB coding region. The recognition sequence of the LexA repressor (SOS box) was identified by a footprinting experiment. It overlaps the -35 sequence of the polB promoter.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=2034216 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Base Sequence; DNA Polymerase II/classification; DNA Polymerase II/genetics; DNA Polymerase II/metabolism; DNA, Bacterial; DNA-Directed DNA Polymerase/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Humans; Molecular Sequence Data; Phylogeny; Promoter Regions, Genetic; Restriction Mapping; Sequence Homology, Nucleic Acid&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2034216&amp;diff=1503637</id>
		<title>PMID:2034216</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2034216&amp;diff=1503637"/>
		<updated>2016-05-10T14:29:53Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:4292146&amp;diff=1503634</id>
		<title>PMID:4292146</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:4292146&amp;diff=1503634"/>
		<updated>2016-05-05T00:43:35Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;W572a9736ab940&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Gershon, H, Schulman, SG and Spevack, AD&#039;&#039;&#039;  (1967) Organic fluorine compounds. 3. Action of perchloryl fluoride on substituted ethyl cyanoacetates and animal toxicities of the fluorinated products. &#039;&#039;J. Med. Chem.&#039;&#039; &#039;&#039;&#039;10&#039;&#039;&#039;:536-41&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
No abstract in PubMed&lt;br /&gt;
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!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=4292146 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Acetates/therapeutic use; Adenocarcinoma/drug therapy; Animals; Carcinoma 256, Walker/drug therapy; Carcinoma, Hepatocellular/drug therapy; Chemistry, Organic; Fluorine/therapeutic use; Leukemia, Experimental/drug therapy; Liver Neoplasms; Lung Neoplasms/drug therapy; Lymphoma/drug therapy; Lymphoma, Non-Hodgkin/drug therapy; Malonates/therapeutic use; Melanoma/drug therapy; Neoplasms, Experimental/drug therapy; Organic Chemistry Phenomena; Sarcoma/drug therapy; Sarcoma 180/drug therapy&lt;br /&gt;
&lt;br /&gt;
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|&amp;lt;span class=&amp;quot;tableEdit_editLink plainlinks&amp;quot;&amp;gt;[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&amp;amp;id=d41d8cd98f00b204e9800998ecf8427e.184461.W572a9736ab940&amp;amp;page=184461&amp;amp;pagename={{FULLPAGENAMEE}}&amp;amp;type=1&amp;amp;template=PMID_info_table edit table]&amp;lt;/span&amp;gt; ||&lt;br /&gt;
|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:4292146&amp;diff=1503633</id>
		<title>PMID:4292146</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:4292146&amp;diff=1503633"/>
		<updated>2016-05-05T00:43:34Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0006563_!_L-serine_metabolic_process&amp;diff=1503632</id>
		<title>Category:GO:0006563 ! L-serine metabolic process</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0006563_!_L-serine_metabolic_process&amp;diff=1503632"/>
		<updated>2016-04-23T13:11:42Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0006563_!_L-serine_metabolic_process}}&lt;br /&gt;
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==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015233_!_pantothenate_transmembrane_transporter_activity&amp;diff=1503631</id>
		<title>Category:GO:0015233 ! pantothenate transmembrane transporter activity</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015233_!_pantothenate_transmembrane_transporter_activity&amp;diff=1503631"/>
		<updated>2016-04-23T12:10:55Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{GO term stub|GO:0015233_!_pantothenate_transmembrane_transporter_activity}}&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:9515930&amp;diff=1503630</id>
		<title>PMID:9515930</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:9515930&amp;diff=1503630"/>
		<updated>2016-04-13T20:01:00Z</updated>

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{|   id=&amp;quot;R570ea57c32699&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Leffers, GG Jr and Gottesman, S&#039;&#039;&#039;  (1998) Lambda Xis degradation in vivo by Lon and FtsH. &#039;&#039;J. Bacteriol.&#039;&#039; &#039;&#039;&#039;180&#039;&#039;&#039;:1573-7&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
Lambda Xis, which is required for site-specific excision of phage lambda from the bacterial chromosome, has a much shorter functional half-life than Int, which is required for both integration and excision (R. A. Weisberg and M. E. Gottesman, p. 489-500, in A. D. Hershey, ed., The Bacteriophage Lambda, 1971). We found that Xis is degraded in vivo by two ATP-dependent proteases, Lon and FtsH (HflB). Xis was stabilized two- to threefold more than in the wild type in a lon mutant and as much as sixfold more in a lon ftsH double mutant at the nonpermissive temperature for the ftsH mutation. Integration of lambda into the bacterial chromosome was delayed in the lon ftsH background, suggesting that accumulation of Xis in vivo interferes with integration. Overexpression of Xis in wild-type cells from a multicopy plasmid inhibited integration of lambda and promoted curing of established lysogens, confirming that accumulation of Xis interferes with the ability of Int to establish and maintain an integrated prophage.&lt;br /&gt;
|-&lt;br /&gt;
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=9515930 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC107061 PMC107061]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
ATP-Dependent Proteases; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage lambda/genetics; Bacteriophage lambda/metabolism; DNA Nucleotidyltransferases/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli/virology; Escherichia coli Proteins; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Lysogeny/genetics; Membrane Proteins/genetics; Membrane Proteins/metabolism; Protease La; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism; Viral Proteins&lt;br /&gt;
&lt;br /&gt;
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|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
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{{LitMaterials}}&lt;br /&gt;
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&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:8990286&amp;diff=1503629</id>
		<title>PMID:8990286</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:8990286&amp;diff=1503629"/>
		<updated>2016-04-13T20:01:00Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;Z570ea57beaba5&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Herman, C, Thévenet, D, D&#039;Ari, R and Bouloc, P&#039;&#039;&#039;  (1997) The HflB protease of Escherichia coli degrades its inhibitor lambda cIII. &#039;&#039;J. Bacteriol.&#039;&#039; &#039;&#039;&#039;179&#039;&#039;&#039;:358-63&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
The cIII protein of bacteriophage lambda is known to protect two regulatory proteins from degradation by the essential Escherichia coli protease HflB (also known as FtsH), viz., the lambda cII protein and the host heat shock sigma factor sigma32. lambda cIII, itself an unstable protein, is partially stabilized when the HflB concentration is decreased, and its half-life is decreased when HflB is overproduced, strongly suggesting that it is degraded by HflB in vivo. The in vivo degradation of lambda cIII (unlike that of sigma32) does not require the molecular chaperone DnaK. Furthermore, the half-life of lambda cIII is not affected by depletion of the endogenous ATP pool, suggesting that lambda cIII degradation is ATP independent (unlike that of lambda cII and sigma32). The lambda cIII protein, which is predicted to contain a 22-amino-acid amphipathic helix, is associated with the membrane, and nonlethal overproduction of lambda cIII makes cells hypersensitive to the detergent sodium dodecyl sulfate. This could reflect a direct lambda cIII-membrane interaction or an indirect association via the membrane-bound HflB protein, which is known to be involved in the assembly of certain periplasmic and outer membrane proteins.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=8990286 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC178704 PMC178704]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
ATP-Dependent Proteases; Adenosine Triphosphate/antagonists &amp;amp; inhibitors; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage lambda/metabolism; Cell Membrane/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Gene Deletion; HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Transcription Factors/metabolism; Viral Proteins&lt;br /&gt;
&lt;br /&gt;
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		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:9515930&amp;diff=1503628</id>
		<title>PMID:9515930</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:9515930&amp;diff=1503628"/>
		<updated>2016-04-13T20:01:00Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:8990286&amp;diff=1503627</id>
		<title>PMID:8990286</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:8990286&amp;diff=1503627"/>
		<updated>2016-04-13T20:00:59Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:3316222&amp;diff=1503624</id>
		<title>PMID:3316222</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:3316222&amp;diff=1503624"/>
		<updated>2016-03-29T08:46:53Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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*   ** PLEASE DON&#039;T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. ** &lt;br /&gt;
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{|   id=&amp;quot;P56fa40fc514cf&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;O&#039;Donnell, ME&#039;&#039;&#039;  (1987) Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli. &#039;&#039;J. Biol. Chem.&#039;&#039; &#039;&#039;&#039;262&#039;&#039;&#039;:16558-65&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
DNA polymerase III holoenzyme was assembled from pure proteins onto a primer template scaffold. The assembly process could be divided into two stages. In the time-consuming first stage, beta subunit and gamma.delta subunit complex were required in forming a tightly bound ATP-activated &amp;quot;preinitiation complex&amp;quot; with a single-stranded DNA bacteriophage circle uniquely primed with a synthetic pentadecadeoxyribonucleotide. This finding substantiates an earlier study using crude protein preparations in a homopolymer system lacking Escherichia coli single-stranded DNA binding protein (Wickner, S. (1976) Proc. Natl. Acad. Sci. U. S. A. 73, 3511-3515). In the second stage, the polymerase III core and the tau subunit rapidly seek out and bind the preinitiation complex to form DNA polymerase III holoenzyme capable of rapid and entirely processive replication of the circular DNA. ATP is not required beyond formation of the preinitiation complex. It is remarkable that the fully assembled DNA polymerase III holoenzyme is so stably bound to the primed DNA circle (4-min half-time of dissociation), yet upon completing a round of synthesis the polymerase cycles within 10 s to a new preinitiation complex on a challenge primed DNA circle. Efficient polymerase cycling only occurred when challenge primed DNA was endowed with a preinitiation complex implying that cycling is mediated by a polymerase subassembly which dissociates from its accessory proteins and associates with a new preinitiation complex. These subunit dynamics suggest mechanisms for polymerase cycling on the lagging strand of replication forks in a growing chromosome.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=3316222 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Adenosine Triphosphate/pharmacology; Adenylyl Imidodiphosphate/pharmacology; Bacterial Proteins/metabolism; Bacteriophages/genetics; DNA Polymerase III/metabolism; DNA, Circular/metabolism; DNA, Single-Stranded/metabolism; DNA, Viral/metabolism; DNA-Directed DNA Polymerase/metabolism; Deoxyadenine Nucleotides/pharmacology; Escherichia coli/enzymology; Escherichia coli/genetics; Multienzyme Complexes/metabolism; Templates, Genetic; Time Factors&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:3316222&amp;diff=1503623</id>
		<title>PMID:3316222</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:3316222&amp;diff=1503623"/>
		<updated>2016-03-29T08:46:52Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:10924523&amp;diff=1503622</id>
		<title>PMID:10924523</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:10924523&amp;diff=1503622"/>
		<updated>2016-03-29T08:16:50Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;S56fa39f2415ba&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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|-&lt;br /&gt;
!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Leu, FP, Hingorani, MM, Turner, J and O&#039;Donnell, M&#039;&#039;&#039;  (2000) The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli. &#039;&#039;J. Biol. Chem.&#039;&#039; &#039;&#039;&#039;275&#039;&#039;&#039;:34609-18&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
In Escherichia coli, the circular beta sliding clamp facilitates processive DNA replication by tethering the polymerase to primer-template DNA. When synthesis is complete, polymerase dissociates from beta and DNA and cycles to a new start site, a primed template loaded with beta. DNA polymerase cycles frequently during lagging strand replication while synthesizing 1-2-kilobase Okazaki fragments. The clamps left behind remain stable on DNA (t(12) approximately 115 min) and must be removed rapidly for reuse at numerous primed sites on the lagging strand. Here we show that delta, a single subunit of DNA polymerase III holoenzyme, opens beta and slips it off DNA (k(unloading) = 0.011 s(-)(1)) at a rate similar to that of the multisubunit gamma complex clamp loader by itself (0.015 s(-)(1)) or within polymerase (pol) III* (0.0065 s(-)(1)). Moreover, unlike gamma complex and pol III*, delta does not require ATP to catalyze clamp unloading. Quantitation of gamma complex subunits (gamma, delta, delta&#039;, chi, psi) in E. coli cells reveals an excess of delta, free from gamma complex and pol III*. Since pol III* and gamma complex occur in much lower quantities and perform several DNA metabolic functions in replication and repair, the delta subunit probably aids beta clamp recycling during DNA replication.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=10924523 PubMed]&lt;br /&gt;
Online version:[http://dx.doi.org/10.1074/jbc.M005495200 10.1074/jbc.M005495200]&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Blotting, Western; DNA Polymerase III/metabolism; DNA Replication; DNA, Bacterial/biosynthesis; DNA, Bacterial/metabolism; Escherichia coli/enzymology&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
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		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:10924523&amp;diff=1503621</id>
		<title>PMID:10924523</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:10924523&amp;diff=1503621"/>
		<updated>2016-03-29T08:16:50Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:1587819&amp;diff=1503620</id>
		<title>PMID:1587819</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:1587819&amp;diff=1503620"/>
		<updated>2016-03-29T07:26:28Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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&amp;lt;!--box uid=d41d8cd98f00b204e9800998ecf8427e.184453.D56fa2e23f1b49--&amp;gt;&lt;br /&gt;
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{|   id=&amp;quot;D56fa2e23f1b49&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Fradkin, LG and Kornberg, A&#039;&#039;&#039;  (1992) Prereplicative complexes of components of DNA polymerase III holoenzyme of Escherichia coli. &#039;&#039;J. Biol. Chem.&#039;&#039; &#039;&#039;&#039;267&#039;&#039;&#039;:10318-22&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
Stepwise reconstitution of the subunits of DNA polymerase III holoenzyme of Escherichia coli offers insights into the organization and function of this multisubunit assembly. A highly processive, holoenzyme-like activity can be generated when the gamma complex, in the presence of ATP and a primed template, activates the beta subunit to form a preinitiation complex, and this is then followed by addition of the core polymerase. Further analysis of early replicative complexes has now revealed: 1) that the gamma complex can stably bind a single-stranded DNA binding protein (SSB)-coated template, 2) that neither SSB coating of the template nor a proper primer terminus is required to form the preinitiation complex, and 3) that the gamma complex stabilizes the preinitiation complex in the presence of ATP and destabilizes it in the presence of adenosine 5&#039;-O-(thiotriphosphate). Based on these findings, a sequence of stages can be formulated for an activation of the beta subunit that enables it to bind the template-primer and thereby interact with the core to create a processive polymerase.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=1587819 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Adenosine Triphosphate/analogs &amp;amp; derivatives; Adenosine Triphosphate/metabolism; DNA Polymerase III/metabolism; DNA Replication; DNA, Bacterial/biosynthesis; Escherichia coli/enzymology; Hydrolysis; Templates, Genetic&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
|&amp;lt;span class=&amp;quot;tableEdit_editLink plainlinks&amp;quot;&amp;gt;[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&amp;amp;id=d41d8cd98f00b204e9800998ecf8427e.184453.D56fa2e23f1b49&amp;amp;page=184453&amp;amp;pagename={{FULLPAGENAMEE}}&amp;amp;type=1&amp;amp;template=PMID_info_table edit table]&amp;lt;/span&amp;gt; ||&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;!--box uid=d41d8cd98f00b204e9800998ecf8427e.184453.D56fa2e23f1b49--&amp;gt;&lt;br /&gt;
&lt;br /&gt;
==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
&lt;br /&gt;
== Useful Materials and Methods {{HelpIcon|Help:Literature}}==&lt;br /&gt;
{{LitMaterials}}&lt;br /&gt;
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&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:1587819&amp;diff=1503619</id>
		<title>PMID:1587819</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:1587819&amp;diff=1503619"/>
		<updated>2016-03-29T07:26:27Z</updated>

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		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:4588736&amp;diff=1503614</id>
		<title>PMID:4588736</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:4588736&amp;diff=1503614"/>
		<updated>2016-03-13T16:19:02Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;M56e592f5dd012&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Kobayashi, M and Ishimoto, M&#039;&#039;&#039;  (1973) Aerobic inhibition of nitrate assimilation in Escherichia coli. &#039;&#039;Z. Allg. Mikrobiol.&#039;&#039; &#039;&#039;&#039;13&#039;&#039;&#039;:405-13&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
No abstract in PubMed&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=4588736 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Aerobiosis; Anaerobiosis; Culture Media; Enterobacter/growth &amp;amp; development; Escherichia coli/enzymology; Escherichia coli/growth &amp;amp; development; Escherichia coli/metabolism; Hydrogen-Ion Concentration; Klebsiella/growth &amp;amp; development; Nitrate Reductases/metabolism; Nitrates/metabolism; Oxygen/pharmacology&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:4588736&amp;diff=1503613</id>
		<title>PMID:4588736</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:4588736&amp;diff=1503613"/>
		<updated>2016-03-13T16:19:01Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2832386&amp;diff=1503604</id>
		<title>PMID:2832386</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2832386&amp;diff=1503604"/>
		<updated>2016-01-13T19:15:36Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{RightTOC}}&lt;br /&gt;
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{|   id=&amp;quot;G5696a2581aff4&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Ishiguro, N and Sato, G&#039;&#039;&#039;  (1988) Nucleotide sequence of insertion sequence IS3411, which flanks the citrate utilization determinant of transposon Tn3411. &#039;&#039;J. Bacteriol.&#039;&#039; &#039;&#039;&#039;170&#039;&#039;&#039;:1902-6&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
The nucleotide sequences of insertion sequences IS3411L (left) and IS3411R (right), present as direct terminal repeats in the citrate utilization of citrate utilization transposon Tn3411, and of IS3411 (generated by intramolecular recombination between IS3411L and IS3411R) were determined. The three IS3411 elements (IS3411R, IS3411L, and IS3411) were 1,309 base pairs long and identical in DNA sequence. IS3411 had 27-base-pair terminal inverted repeats with three bases mismatched and one long open reading frame (240 amino acids) that was proposed to be a transposase. Three polypeptides of 29,000, 27,000, and about 10,000 molecular weight, determined by IS3411, were identified in minicells. Since Tn3411 generates a 3-base-pair repeat upon integration, the nucleotide sequences of IS3411 were compared with those of IS3.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=2832386 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC211048 PMC211048]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Base Sequence; Citrates/metabolism; DNA Transposable Elements; DNA, Bacterial/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Molecular Sequence Data; Mutation; Plasmids; Repetitive Sequences, Nucleic Acid&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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|}&lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2832386&amp;diff=1503603</id>
		<title>PMID:2832386</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2832386&amp;diff=1503603"/>
		<updated>2016-01-13T19:15:36Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0042936_!_dipeptide_transporter_activity&amp;diff=1503600</id>
		<title>Category:GO:0042936 ! dipeptide transporter activity</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0042936_!_dipeptide_transporter_activity&amp;diff=1503600"/>
		<updated>2015-12-07T06:59:40Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0042936_!_dipeptide_transporter_activity}}&lt;br /&gt;
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==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015116_!_sulfate_transmembrane_transporter_activity&amp;diff=1503599</id>
		<title>Category:GO:0015116 ! sulfate transmembrane transporter activity</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015116_!_sulfate_transmembrane_transporter_activity&amp;diff=1503599"/>
		<updated>2015-12-07T05:59:15Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{GO term stub|GO:0015116_!_sulfate_transmembrane_transporter_activity}}&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015794_!_glycerol-3-phosphate_transport&amp;diff=1503598</id>
		<title>Category:GO:0015794 ! glycerol-3-phosphate transport</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015794_!_glycerol-3-phosphate_transport&amp;diff=1503598"/>
		<updated>2015-12-07T05:59:14Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0015794_!_glycerol-3-phosphate_transport}}&lt;br /&gt;
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==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0045717_!_negative_regulation_of_fatty_acid_biosynthetic_process&amp;diff=1503597</id>
		<title>Category:GO:0045717 ! negative regulation of fatty acid biosynthetic process</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0045717_!_negative_regulation_of_fatty_acid_biosynthetic_process&amp;diff=1503597"/>
		<updated>2015-12-07T05:59:14Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0045717_!_negative_regulation_of_fatty_acid_biosynthetic_process}}&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0019064_!_fusion_of_virus_membrane_with_host_plasma_membrane&amp;diff=1503596</id>
		<title>Category:GO:0019064 ! fusion of virus membrane with host plasma membrane</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0019064_!_fusion_of_virus_membrane_with_host_plasma_membrane&amp;diff=1503596"/>
		<updated>2015-12-07T05:28:53Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0019064_!_fusion_of_virus_membrane_with_host_plasma_membrane}}&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0042907_!_xanthine_transmembrane_transporter_activity&amp;diff=1503595</id>
		<title>Category:GO:0042907 ! xanthine transmembrane transporter activity</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0042907_!_xanthine_transmembrane_transporter_activity&amp;diff=1503595"/>
		<updated>2015-12-07T05:28:53Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0042907_!_xanthine_transmembrane_transporter_activity}}&lt;br /&gt;
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==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
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		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015774_!_polysaccharide_transport&amp;diff=1503594</id>
		<title>Category:GO:0015774 ! polysaccharide transport</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0015774_!_polysaccharide_transport&amp;diff=1503594"/>
		<updated>2015-12-07T05:28:52Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{GO term stub|GO:0015774_!_polysaccharide_transport}}&lt;br /&gt;
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==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:3003520&amp;diff=1503592</id>
		<title>PMID:3003520</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:3003520&amp;diff=1503592"/>
		<updated>2015-11-27T16:06:27Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;P56587f83232a4&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Fukuda, R, Yano, R, Fukui, T, Hase, T, Ishihama, A and Matsubara, H&#039;&#039;&#039;  (1985) Cloning of the Escherichia coli gene for the stringent starvation protein. &#039;&#039;Mol. Gen. Genet.&#039;&#039; &#039;&#039;&#039;201&#039;&#039;&#039;:151-7&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
In order to clone the Escherichia coli gene for the stringent starvation protein (SSP), we determined its N-terminal sequence as well as the sequence of two peptide fragments obtained by cyanogen bromide cleavage of the protein. We then chemically synthesized four sets of oligodeoxyribonucleotide mixtures that represented possible codon combinations for parts of these amino acid sequences. The synthetic oligonucleotides were labelled with 32P at their 5&#039;-termini and used as hybridization probes to detect DNA fragments containing the complementary sequences. Genomic Southern hybridization of E. coli chromosomal DNA gave up to ten DNA fragments hybridizing with each probe but only a few hybridized with two or more of the probes. The latter fragments were cloned in pBR322. By determining partial base sequences with a rapid method and examining proteins encoded by the DNA fragments, we were able to show that we had isolated a clone containing the complete SSP structural gene.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=3003520 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA Restriction Enzymes; DNA, Superhelical/genetics; Escherichia coli/genetics; GTP Pyrophosphokinase/genetics; Genes; Genes, Bacterial; Nucleic Acid Hybridization; Phosphotransferases/genetics; Plasmids&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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|}&lt;br /&gt;
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&lt;br /&gt;
==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:3003520&amp;diff=1503591</id>
		<title>PMID:3003520</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:3003520&amp;diff=1503591"/>
		<updated>2015-11-27T16:06:26Z</updated>

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		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:8858586&amp;diff=1503590</id>
		<title>PMID:8858586</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:8858586&amp;diff=1503590"/>
		<updated>2015-11-26T11:29:10Z</updated>

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{|   id=&amp;quot;I5656ed0530848&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Wang, X and Lutkenhaus, J&#039;&#039;&#039;  (1996) FtsZ ring: the eubacterial division apparatus conserved in archaebacteria. &#039;&#039;Mol. Microbiol.&#039;&#039; &#039;&#039;&#039;21&#039;&#039;&#039;:313-9&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
FtsZ is a tubulin-like protein that is essential for cell division in eubacteria. It functions by forming a ring at the division site that directs septation. The archaebacteria constitute a kingdom of life separate from eubacteria and eukaryotes. Like eubacteria, archaebacteria are prokaryotes, although they are phylogenetically closer to eukaryotes. Here it is shown that archaebacteria also possess FtsZ and that it is biochemically similar to eubacterial FtsZs. Significantly, FtsZ from the archaebacterium Haloferax volcanii is a GTPase that is localized to a ring that coincides with the division constriction. These results indicate that the FtsZ ring was part of the division apparatus of a common prokaryotic ancestor that was retained by both eubacteria and archaebacteria.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=8858586 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Archaea/cytology; Archaea/genetics; Archaea/physiology; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Base Sequence; Cell Division/genetics; Cell Division/physiology; Conserved Sequence; Cytoskeletal Proteins; DNA, Bacterial/genetics; Escherichia coli/genetics; GTP Phosphohydrolases/genetics; GTP Phosphohydrolases/physiology; Halobacteriaceae/cytology; Halobacteriaceae/genetics; Halobacteriaceae/physiology; Methanobacterium/cytology; Methanobacterium/genetics; Methanobacterium/physiology; Molecular Sequence Data; Sequence Homology, Amino Acid; Species Specificity; Tubulin/genetics; Tubulin/physiology&lt;br /&gt;
&lt;br /&gt;
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&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:8858586&amp;diff=1503589</id>
		<title>PMID:8858586</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:8858586&amp;diff=1503589"/>
		<updated>2015-11-26T11:29:09Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:365579&amp;diff=1503568</id>
		<title>PMID:365579</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:365579&amp;diff=1503568"/>
		<updated>2015-10-03T12:29:34Z</updated>

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{|   id=&amp;quot;S560fca2e6378d&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Muranova, TA, Muranov, AV, Markova, LF and Ovchinnikov, YA&#039;&#039;&#039;  (1978) The primary structure of ribosomal protein L3 from Escherichia coli 70 S ribosomes. &#039;&#039;FEBS Lett.&#039;&#039; &#039;&#039;&#039;96&#039;&#039;&#039;:301-5&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
No abstract in PubMed&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=365579 PubMed]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Bacterial Proteins; Escherichia coli; Glutamine/analogs &amp;amp; derivatives; Glutamine/analysis; Peptide Fragments/analysis; Ribosomal Proteins&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:365579&amp;diff=1503567</id>
		<title>PMID:365579</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:365579&amp;diff=1503567"/>
		<updated>2015-10-03T12:29:34Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0016959_!_class_I_ribonucleotide_reductase_activity&amp;diff=1503553</id>
		<title>Category:GO:0016959 ! class I ribonucleotide reductase activity</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0016959_!_class_I_ribonucleotide_reductase_activity&amp;diff=1503553"/>
		<updated>2015-09-19T10:59:30Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{GO term stub|GO:0016959_!_class_I_ribonucleotide_reductase_activity}}&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0045941_!_positive_regulation_of_cellular_transcription&amp;diff=1503552</id>
		<title>Category:GO:0045941 ! positive regulation of cellular transcription</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0045941_!_positive_regulation_of_cellular_transcription&amp;diff=1503552"/>
		<updated>2015-09-19T10:59:29Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;{{GO term stub|GO:0045941_!_positive_regulation_of_cellular_transcription}}&lt;br /&gt;
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==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0043847_!_DNA_polymerase_III,_clamp_loader_chi/psi_subcomplex&amp;diff=1503475</id>
		<title>Category:GO:0043847 ! DNA polymerase III, clamp loader chi/psi subcomplex</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0043847_!_DNA_polymerase_III,_clamp_loader_chi/psi_subcomplex&amp;diff=1503475"/>
		<updated>2015-08-28T17:32:24Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New GO term category page&lt;/p&gt;
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&lt;div&gt;{{GO term stub|GO:0043847_!_DNA_polymerase_III,_clamp_loader_chi/psi_subcomplex}}&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2644231&amp;diff=1503458</id>
		<title>PMID:2644231</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2644231&amp;diff=1503458"/>
		<updated>2015-08-07T16:24:06Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: Fill PMID: Page!&lt;/p&gt;
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{|   id=&amp;quot;A55c4dba56ade3&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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!align=left  |Citation&lt;br /&gt;
||&lt;br /&gt;
&#039;&#039;&#039;Sadosky, AB, Davidson, A, Lin, RJ and Hill, CW&#039;&#039;&#039;  (1989) rhs gene family of Escherichia coli K-12. &#039;&#039;J. Bacteriol.&#039;&#039; &#039;&#039;&#039;171&#039;&#039;&#039;:636-42&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
Two additional members of a novel Escherichia coli gene family, the rhs genes, have been cloned and characterized. The structures of these loci, rhsC and rhsD, have been compared with those of rhsA and rhsB. All four loci contain a homologous 3.7-kilobase-pair core. Sequence comparison of the first 300 nucleotides of the cores showed that rhsA, rhsB, and rhsC are closely related, with only 1 to 2% sequence divergence, whereas rhsD is 18% divergent from the others. The beginning of the core coincides with the initiation of an open reading frame that extends beyond the 300 nucleotides compared. Whether a protein product is produced from this open reading frame has not been established. However, nucleotide substitutions which differentiate the cores have highly conservative effects on the predicted protein products; this suggests that products are made from the open reading frame and are under severe selection. The four rhs loci have been placed on both the genetic and restriction maps of E. coli K-12. A fifth rhs locus remains to be characterized. In terms of size, number, and sequence conservation, the rhs genes make up one of the most significant repetitions in E. coli, comparable to the rRNA operons.&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Links&lt;br /&gt;
||&lt;br /&gt;
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=2644231 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC209644 PMC209644]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Amino Acid Sequence; Base Sequence; Cloning, Molecular; Escherichia coli/genetics; Genes, Bacterial; Molecular Sequence Data; Multigene Family; Plasmids; Restriction Mapping&lt;br /&gt;
&lt;br /&gt;
|- class=&amp;quot;tableEdit_footer&amp;quot; &lt;br /&gt;
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==Significance {{HelpIcon|Help:Literature}} ==&lt;br /&gt;
{{LitSignificance}}&lt;br /&gt;
&lt;br /&gt;
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{{LitMaterials}}&lt;br /&gt;
&lt;br /&gt;
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&lt;br /&gt;
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{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:2644231&amp;diff=1503457</id>
		<title>PMID:2644231</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:2644231&amp;diff=1503457"/>
		<updated>2015-08-07T16:24:05Z</updated>

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	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:10992475&amp;diff=1503430</id>
		<title>PMID:10992475</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:10992475&amp;diff=1503430"/>
		<updated>2015-08-05T10:56:06Z</updated>

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{|   id=&amp;quot;P55c1ebc4a583b&amp;quot;  class=&amp;quot; tableEdit PMID_info_table&amp;quot;  &lt;br /&gt;
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&#039;&#039;&#039;McVeigh, A, Fasano, A, Scott, DA, Jelacic, S, Moseley, SL, Robertson, DC and Savarino, SJ&#039;&#039;&#039;  (2000) IS1414, an Escherichia coli insertion sequence with a heat-stable enterotoxin gene embedded in a transposase-like gene. &#039;&#039;Infect. Immun.&#039;&#039; &#039;&#039;&#039;68&#039;&#039;&#039;:5710-5&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Abstract&lt;br /&gt;
||&lt;br /&gt;
Enteroaggregative Escherichia coli (EAEC) heat-stable enterotoxin 1 (EAST1) was originally discovered in EAEC but has also been associated with enterotoxigenic E. coli (ETEC). Multiple genomic restriction fragments from each of three ETEC strains of human origin showed homology with an EAST1 gene probe. A single hybridizing fragment was detected on the plasmid of ETEC strain 27D that also encodes heat-stable enterotoxin Ib and colonization factor antigen I. We isolated and characterized this fragment, showing that it (i) carries an allele of astA nearly identical to that originally reported from EAEC 17-2 and (ii) expressed enterotoxic activity. Sequence analysis of the toxin coding region revealed that astA is completely embedded within a 1,209-bp open reading frame (ORF1), whose coding sequence is on the same strand but in the -1 reading frame in reference to the toxin gene. In vitro expression of the predicted M(r)- approximately 46,000 protein product of ORF1 was demonstrated. ORF1 is highly similar to transposase genes of IS285 from Yersinia pestis, IS1356 from Burkholderia cepacia, and ISRm3 from Rhizobium meliloti. It is bounded by 30-bp imperfect inverted repeat sequences and flanked by 8-bp direct repeats. Based on these structural features, pathognomonic of a regular insertion sequence, this element was designated IS1414. Preliminary experiments to show IS1414 translocation were unsuccessful. Overlapping genes of the type suggested by the IS1414 core region have heretofore not been described in bacteria. It seems to offer a most efficient mechanism for intragenomic and horizontal dissemination of EAST1.&lt;br /&gt;
|-&lt;br /&gt;
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;amp;db=pubmed&amp;amp;dopt=Abstract&amp;amp;list_uids=10992475 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC101527 PMC101527]&lt;br /&gt;
&lt;br /&gt;
|-&lt;br /&gt;
!align=left  |Keywords&lt;br /&gt;
||&lt;br /&gt;
Alleles; Amino Acid Sequence; Animals; Bacterial Toxins/genetics; Bacterial Toxins/metabolism; Bacterial Toxins/toxicity; Base Sequence; DNA Transposable Elements; Enterotoxins/genetics; Enterotoxins/metabolism; Enterotoxins/toxicity; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli/pathogenicity; Gene Dosage; Genes, Bacterial; Humans; Ileum; Mice; Molecular Sequence Data; Phenotype; Plasmids; Rabbits; Sequence Analysis, DNA; Transposases/genetics; Transposases/metabolism; Virulence/genetics&lt;br /&gt;
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==See also==&lt;br /&gt;
&lt;br /&gt;
==References==&lt;br /&gt;
{{RefHelp}}&lt;br /&gt;
&amp;lt;references/&amp;gt;&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
	<entry>
		<id>https://ecoliwiki.org/colipedia/index.php?title=PMID:10992475&amp;diff=1503429</id>
		<title>PMID:10992475</title>
		<link rel="alternate" type="text/html" href="https://ecoliwiki.org/colipedia/index.php?title=PMID:10992475&amp;diff=1503429"/>
		<updated>2015-08-05T10:56:04Z</updated>

		<summary type="html">&lt;p&gt;38.100.21.109: New PMID: Page!&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;PMID on Demand placeholder&lt;/div&gt;</summary>
		<author><name>38.100.21.109</name></author>
	</entry>
</feed>