EcoliWiki - User contributions [en]

https://ecoliwiki.org/colipedia/api.php?action=feedcontributions&feedformat=atom&user=5.9.72.48 EcoliWiki - User contributions [en] 2026-11-04T16:00:13Z User contributions MediaWiki 1.43.11 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0042937_!_tripeptide_transporter_activity&diff=1504192 Category:GO:0042937 ! tripeptide transporter activity 2016-07-07T07:47:03Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0042937_!_tripeptide_transporter_activity}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8294007&diff=1504191 PMID:8294007 2016-07-07T07:39:27Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="F577e072eacad0" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Dong, J, Iuchi, S, Kwan, HS, Lu, Z and Lin, EC''' (1993) The deduced amino-acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli. ''Gene'' '''136''':227-30<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The cpxA gene of Escherichia coli K-12 encodes a membrane-associated sensor element of a two-component signal transduction system in bacteria. The cognate regulator element, however, has not yet been definitively identified. A 2.1-kb segment upstream from cpxA was amplified by polymerase chain reaction, cloned and sequenced. An open reading frame encoding 232 amino acids was found. It showed high homology to the regulator elements of two-component transduction systems. The newly identified gene, designated as cpxR, may encode the cognate protein receiving signals from CpxA.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8294007 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Cloning, Molecular; DNA, Bacterial; Escherichia coli/genetics; Molecular Sequence Data; Sequence Homology, Amino Acid; Signal Transduction<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184773.F577e072eacad0&page=184773&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8294007&diff=1504190 PMID:8294007 2016-07-07T07:39:26Z

<p>5.9.72.48: New PMID: Page!</p> <hr /> <div>PMID on Demand placeholder</div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:2544445&diff=1504189 PMID:2544445 2016-07-07T07:39:26Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="E577e072dae66e" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Puustinen, A, Finel, M, Virkki, M and Wikström, M''' (1989) Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. ''FEBS Lett.'' '''249''':163-7<br /> |-<br /> !align=left |Abstract<br /> ||<br /> Spheroplasts from aerobically grown wild-type Paracoccus denitrificans cells respire with succinate despite specific inhibition of the cytochrome bc1 complex by myxothiazol. Coupled to this activity, which involves only b-type cytochromes, there is translocation of 1.5-1.9 h+/e- across the cytoplasmic membrane. Similar H+ translocation ratios are observed during oxidation of ubiquinol in spheroplasts from aerobically grown mutants of Paracoccus lacking cytochrome c oxidase, or deficient in cytochrome c, as well as in a strain of E. coli from which cytochrome d was deleted. These observations show that the cytochrome o complex is a proton pump much like cytochrome aa3 to which it is structurally related.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2544445 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Cytochrome b Group; Cytochromes/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Oxidation-Reduction; Oxygen Consumption; Paracoccus denitrificans/enzymology; Protons; Spheroplasts/enzymology; Ubiquinone/analogs & derivatives; Ubiquinone/metabolism<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184772.E577e072dae66e&page=184772&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:2544445&diff=1504188 PMID:2544445 2016-07-07T07:39:25Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0010038_!_response_to_metal_ion&diff=1504187 Category:GO:0010038 ! response to metal ion 2016-07-07T07:39:25Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0010038_!_response_to_metal_ion}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0043200_!_response_to_amino_acid&diff=1504186 Category:GO:0043200 ! response to amino acid 2016-07-07T07:24:57Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0043200_!_response_to_amino_acid}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8801423&diff=1504185 PMID:8801423 2016-07-07T06:33:34Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="X577df7bdaeb76" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Ardourel, M, Lortet, G, Maillet, F, Roche, P, Truchet, G, Promé, JC and Rosenberg, C''' (1995) In Rhizobium meliloti, the operon associated with the nod box n5 comprises nodL, noeA and noeB, three host-range genes specifically required for the nodulation of particular Medicago species. ''Mol. Microbiol.'' '''17''':687-99<br /> |-<br /> !align=left |Abstract<br /> ||<br /> In Rhizobium meliloti, the genes required for nodulation of legume hosts are under the control of DNA regulatory sequences called nod boxes. In this paper, we have characterized three host-specific nodulation genes, which form a flavonoid-inducible operon down-stream of the nod box n5. The first gene of this operon is identical to the nodL gene identified by Baev and Kondorosi (1992) in R. meliloti strain AK631. The product of the second gene, NoeA, presents some homology with a methyltransferase. nodL mutants synthesize Nod factors lacking the O-acetate substituent. In contrast, in strains carrying a mutation in either noeA or noeB, no modification in Nod-factor structure or production could be detected. On particular hosts, such as Medicago littoralis, mutants of the n5 operon showed a very weak nodule-forming ability, associated with a drastic decrease in the number of infection threads, while nodulation of Medicago truncatula or Melilotus alba was not affected. Thus, nodL noeA and noeB are host-specific nodulation genes. By using a gain-of-function approach, we showed that the presence of nodL, and hence of O-acetylated Nod factors, is a major prerequisite for confering the ability to nodulate alfalfa upon the heterologous bacterium Rhizobium tropici.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8801423 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Acetylation; Acetyltransferases/genetics; Amino Acid Sequence; Bacterial Proteins/genetics; Carbohydrate Sequence; Chromosome Mapping; Genes, Bacterial/genetics; Lipopolysaccharides/biosynthesis; Lipopolysaccharides/chemistry; Medicago sativa/microbiology; Molecular Sequence Data; Open Reading Frames; Operon; Plant Roots/microbiology; Regulatory Sequences, Nucleic Acid; Regulon; Sequence Analysis, DNA; Sinorhizobium meliloti/genetics; Species Specificity; Symbiosis<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184769.X577df7bdaeb76&page=184769&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8801423&diff=1504184 PMID:8801423 2016-07-07T06:33:33Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=User:Sujayc&diff=1504183 User:Sujayc 2016-07-07T04:27:41Z

<p>5.9.72.48: Fill User: Page!</p> <hr /> <div>Click "edit table" in the last row to add information to the table. Click [[Help:Adding_your_information|here]] to find out how to add more information to your user page. <br /> <br /> <br /> <br /> {| id="T577dda3dc691a" class=" tableEdit User_info_table" <br /> <br /> |-<br /> !align=left |Name (Last, First)<br /> |-<br /> !align=left |Organization<br /> |-<br /> !align=left |Position<br /> |-<br /> !align=left |Address<br /> |-<br /> !align=left |Contact Info<br /> |-<br /> !align=left |Website(s)<br /> |-<br /> !align=left |Interests<br /> |-<br /> !align=left |Genes<br /> |-<br /> !align=left |Lab members<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184768.T577dda3dc691a&page=184768&pagename={{FULLPAGENAMEE}}&type=1&template=User_info_table edit table]</span><br /> |}<br /> <br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=User:Sujayc&diff=1504182 User:Sujayc 2016-07-07T04:27:41Z

<p>5.9.72.48: New User: Page!</p> <hr /> <div></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:342519&diff=1504181 PMID:342519 2016-07-07T03:40:52Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="C577dcf446c627" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Reiners, JJ Jr, Messenger, LJ and Zalkin, H''' (1978) Immunological cross-reactivity of Escherichia coli anthranilate synthetase, glutamate synthase, and other proteins. ''J. Biol. Chem.'' '''253''':1226-33<br /> |-<br /> !align=left |Abstract<br /> ||<br /> No abstract in PubMed<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=342519 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Anthranilate Synthase/immunology; Anthranilate Synthase/isolation & purification; Antibodies; Bacterial Proteins/immunology; Bacterial Proteins/isolation & purification; Complement Fixation Tests; Cross Reactions; Escherichia coli/enzymology; Glutamate Synthase/immunology; Glutamate Synthase/isolation & purification; Precipitin Tests; Radioimmunoassay; Transaminases/immunology<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184767.C577dcf446c627&page=184767&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:342519&diff=1504180 PMID:342519 2016-07-07T03:40:52Z

<p>5.9.72.48: New PMID: Page!</p> <hr /> <div>PMID on Demand placeholder</div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:1669732&diff=1504179 PMID:1669732 2016-07-07T03:38:13Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="U577dcea53cbc6" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Knoll, M''' (1991) [In Maria's life there are others who set the tempo. Interview by Carina Roxström]. ''Vardfacket'' '''15''':8-15<br /> |-<br /> !align=left |Abstract<br /> ||<br /> No abstract in PubMed<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1669732 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Adult; Child; Child Rearing; Family; Female; Humans; Life Style; Nurses; Women, Working<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.180698.U577dcea53cbc6&page=180698&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:6194415&diff=1504178 PMID:6194415 2016-07-07T02:33:34Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="V577dbf7e4c569" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Filutowicz, M and Jonczyk, P''' (1983) The gyrB gene product functions in both initiation and chain polymerization of Escherichia coli chromosome replication: suppression of the initiation deficiency in gyrB-ts mutants by a class of rpoB mutations. ''Mol. Gen. Genet.'' '''191''':282-7<br /> |-<br /> !align=left |Abstract<br /> ||<br /> A class of rpoB mutations is described which suppresses replication and transcription deficiency in gyrB-ts mutants shifted to a nonpermissive temperature. The compensatory effect of an altered subunit B of RNA polymerase (rpoB) for the gyrB defect, indicates that transcription is a primary target of the B subunit of DNA gyrase. One gyrB mutation (gyrB402-ts) shows deficiency in chromosome elongation at the nonpermissive temperature, both in vivo and in cells permeabilized with toluene. It is therefore concluded that the gyrB polypeptide functions at least dually in replication; first, at the level of transcription initiation and second, at the level of chain polymerization.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6194415 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> DNA Replication; DNA Topoisomerases, Type II/genetics; DNA, Bacterial/biosynthesis; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Bacterial; Mutation; RNA, Bacterial/biosynthesis; Suppression, Genetic; Temperature; Transcription, Genetic<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184765.V577dbf7e4c569&page=184765&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:6194415&diff=1504177 PMID:6194415 2016-07-07T02:33:34Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0051304_!_chromosome_separation&diff=1504176 Category:GO:0051304 ! chromosome separation 2016-07-07T02:33:33Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0051304_!_chromosome_separation}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0051276_!_chromosome_organization&diff=1504175 Category:GO:0051276 ! chromosome organization 2016-07-07T02:33:32Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0051276_!_chromosome_organization}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0032153_!_cell_division_site&diff=1504174 Category:GO:0032153 ! cell division site 2016-07-07T02:33:32Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0032153_!_cell_division_site}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0019836_!_hemolysis_by_symbiont_of_host_erythrocytes&diff=1504173 Category:GO:0019836 ! hemolysis by symbiont of host erythrocytes 2016-07-07T02:33:31Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0019836_!_hemolysis_by_symbiont_of_host_erythrocytes}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0008997_!_ribonuclease_R_activity&diff=1504172 Category:GO:0008997 ! ribonuclease R activity 2016-07-07T02:33:30Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0008997_!_ribonuclease_R_activity}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=Category:GO:0009651_!_response_to_salt_stress&diff=1504171 Category:GO:0009651 ! response to salt stress 2016-07-07T02:12:08Z

<p>5.9.72.48: New GO term category page</p> <hr /> <div>{{GO term stub|GO:0009651_!_response_to_salt_stress}}<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9915704&diff=1504170 PMID:9915704 2016-07-07T02:05:30Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="M577db8ea48c46" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Rodionov, O, Lobocka, M and Yarmolinsky, M''' (1999) Silencing of genes flanking the P1 plasmid centromere. ''Science'' '''283''':546-9<br /> |-<br /> !align=left |Abstract<br /> ||<br /> Partition modules stabilize bacterial plasmids and chromosomes by actively promoting their segregation into daughter cells. The partition module of plasmid P1 is typical and consists of a centromere site, parS, and genes that encode proteins ParA and ParB. We show that ParB can silence genes flanking parS (to which ParB binds), apparently by polymerizing along the DNA from a nucleation site at parS. Wild-type ParB contacts an extensive region of P1 DNA; silencing-defective ParB proteins, which were found to be partition-defective, are less able to spread. Hence, the silenced structure appears to function in partitioning.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9915704 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Centromere/physiology; Cross-Linking Reagents; DNA Helicases; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; DNA-Binding Proteins; Escherichia coli/genetics; Formaldehyde; Gene Expression Regulation, Bacterial; Genes, Reporter; Mutation; Plasmids/genetics; Plasmids/physiology; Proteins/genetics; Proteins/metabolism; Repressor Proteins/genetics; Repressor Proteins/metabolism; Trans-Activators<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184758.M577db8ea48c46&page=184758&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9915704&diff=1504169 PMID:9915704 2016-07-07T02:05:30Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9288963&diff=1504168 PMID:9288963 2016-07-07T02:05:29Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="Q577db8e99cc29" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Guo, F, Gopaul, DN and van Duyne, GD''' (1997) Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. ''Nature'' '''389''':40-6<br /> |-<br /> !align=left |Abstract<br /> ||<br /> During site-specific DNA recombination, which brings about genetic rearrangement in processes such as viral integration and excision and chromosomal segregation, recombinase enzymes recognize specific DNA sequences and catalyse the reciprocal exchange of DNA strands between these sites. The bacteriophage recombinase Cre catalyses site-specific recombination between two 34-base-pair loxP sites. The crystal structure at 2.4 A resolution of Cre bound to a loxP substrate reveals an intermediate in the recombination reaction, in which a Cre molecule has cleaved the substrate to form a covalent 3'-phosphotyrosine linkage with the DNA. Four recombinases and two loxP sites form a synapsed structure in which the DNA resembles models of four-way Holliday-Junction intermediates. The Cre-loxP complex challenges models of site-specific recombination that require large changes in quaternary structure. Subtle allosteric changes at the carboxy termini of the Cre subunits may instead coordinate the cleavage and strand-exchange reactions.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9288963 PubMed]<br /> Online version:[http://dx.doi.org/10.1038/37925 10.1038/37925]<br /> |-<br /> !align=left |Keywords<br /> ||<br /> Amino Acid Sequence; Binding Sites; DNA/chemistry; DNA/metabolism; Escherichia coli; Integrases/chemistry; Integrases/genetics; Integrases/metabolism; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Phosphotyrosine/chemistry; Phosphotyrosine/metabolism; Protein Conformation; Protein Folding; Recombinant Proteins/chemistry; Recombination, Genetic; Viral Proteins<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184757.Q577db8e99cc29&page=184757&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9288963&diff=1504167 PMID:9288963 2016-07-07T02:05:29Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9182555&diff=1504166 PMID:9182555 2016-07-07T02:05:29Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="C577db8e8f1a58" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Davey, MJ and Funnell, BE''' (1997) Modulation of the P1 plasmid partition protein ParA by ATP, ADP, and P1 ParB. ''J. Biol. Chem.'' '''272''':15286-92<br /> |-<br /> !align=left |Abstract<br /> ||<br /> ParA is an essential P1 plasmid partition protein. It represses transcription of the par genes (parA and parB) and is also required for a second, as yet undefined step in partition. ParA is a ParB-stimulated ATPase that binds to a specific DNA site in the par promoter region. ATP binding and hydrolysis by ParA affect ParA activities in vitro. ATP and ADP binding stimulate ParA DNA binding and dimerization; however, ATP hydrolysis has a negative effect on DNA binding. Our current experiments reveal that ATP binding and hydrolysis affect ParA conformation and ParA sensitivity to ParB. Nucleotide binding assays show that ParA binds ATP better than ADP (Kd values of 33 and 50 microM, respectively). Interaction with these nucleotides as well as ATP hydrolysis by ParA alter ParA conformation as established by CD and ParA sensitivity to heat denaturation. Finally, we show that ParB stimulates ParA DNA binding. This stimulation requires ATP hydrolysis in vitro, suggesting that one role for ATP hydrolysis in vivo is to make ParA repressor sensitive to ParB. Our observations lead to the suggestion that ATP binding and hydrolysis have separable roles in ParA repressor function and perhaps in ParA partition functions as well.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9182555 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Adenosine Diphosphate/metabolism; Adenosine Triphosphate/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; DNA-Binding Proteins/metabolism; Hydrolysis; Plasmids; Protein Binding; Protein Conformation<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184756.C577db8e8f1a58&page=184756&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9182555&diff=1504165 PMID:9182555 2016-07-07T02:05:28Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9082984&diff=1504164 PMID:9082984 2016-07-07T02:05:28Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="B577db8e85cdaf" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Kwon, HJ, Tirumalai, R, Landy, A and Ellenberger, T''' (1997) Flexibility in DNA recombination: structure of the lambda integrase catalytic core. ''Science'' '''276''':126-31<br /> |-<br /> !align=left |Abstract<br /> ||<br /> Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr342 is attached to the 3'-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr342 nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9082984 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1839824 PMC1839824]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Amino Acid Sequence; Attachment Sites, Microbiological; Bacteriophage lambda/enzymology; Binding Sites; Cloning, Molecular; Conserved Sequence; Crystallography, X-Ray; DNA/metabolism; DNA Nucleotidyltransferases/chemistry; DNA Nucleotidyltransferases/metabolism; Hydrogen Bonding; Integrases/chemistry; Integrases/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Folding; Protein Structure, Secondary; Recombinases; Recombination, Genetic; Tyrosine/chemistry; Tyrosine/metabolism; Virus Integration<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184755.B577db8e85cdaf&page=184755&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:9082984&diff=1504163 PMID:9082984 2016-07-07T02:05:28Z

<p>5.9.72.48: New PMID: Page!</p> <hr /> <div>PMID on Demand placeholder</div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8702525&diff=1504162 PMID:8702525 2016-07-07T02:05:27Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="H577db8e7bd867" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Magnuson, R, Lehnherr, H, Mukhopadhyay, G and Yarmolinsky, MB''' (1996) Autoregulation of the plasmid addiction operon of bacteriophage P1. ''J. Biol. Chem.'' '''271''':18705-10<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The P1 plasmid addiction operon increases the apparent stability of a plasmid that carries it by killing plasmid-free (cured) segregants. The operon consists of a gene encoding an endotoxin responsible for death on curing (doc), preceded by a gene encoding a relatively unstable antidote that can prevent host death (phd). When the copy number of the operon was increased, expression of a lacZ reporter fused to the promoter of the operon decreased, indicating that expression of the operon was stabilized by an autoregulatory circuit. Transcription of the lacZ reporter was repressed about 10-fold when phd, without doc, was expressed from an exogenous promoter. DNase I footprinting showed that Phd binds a perfect 10-base pair palindromic DNA sequence and, at higher concentrations, an adjacent, imperfect palindrome. The palindromic sites are located between the -10 region of the putative promoter and the start codon of phd. Electrophoretic mobility of DNA containing the promoter region was retarded in the presence of Phd and further retarded in the presence of Phd and Doc. When doc was co-expressed with phd, repression of the lacZ fusion was enhanced more than 100-fold. Thus, both products of the addiction operon participate in its autoregulation.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8702525 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Bacteriophage P1/genetics; Bacteriophage P1/physiology; Base Sequence; Binding Sites/genetics; Cloning, Molecular; DNA Primers/genetics; DNA, Viral/genetics; DNA, Viral/metabolism; Deoxyribonuclease I; Gene Expression Regulation, Viral; Genes, Reporter; Genes, Viral; Homeostasis/genetics; Homeostasis/physiology; Lac Operon; Molecular Sequence Data; Operon; Plasmids/genetics; Viral Proteins/genetics; Viral Proteins/isolation & purification; Viral Proteins/physiology<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184754.H577db8e7bd867&page=184754&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8702525&diff=1504161 PMID:8702525 2016-07-07T02:05:27Z

<p>5.9.72.48: New PMID: Page!</p> <hr /> <div>PMID on Demand placeholder</div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8676375&diff=1504160 PMID:8676375 2016-07-07T02:05:25Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="J577db8e564d47" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Lobocka, M and Yarmolinsky, M''' (1996) P1 plasmid partition: a mutational analysis of ParB. ''J. Mol. Biol.'' '''259''':366-82<br /> |-<br /> !align=left |Abstract<br /> ||<br /> P1 plasmid partition to daughter cells requires plasmid proteins, ParA and ParB, and a centromere analog, parS, to which ParB binds. ParA and ParB decrease the loss frequencies of some low copy number plasmid vectors with parS inserts, as well as that of P1 itself, more than 100-fold. Unexpectedly, we find that Par proteins can actively destabilize other parS-plasmid constructs under similar conditions. Only ParB is required for this partition dysfunction. The destabilization can be dramatic; certain parS-plasmid constructs cannot even be maintained in the presence of ParB. We take advantage of this partition dysfunction to select parB mutants unable to destabilize a particularly ParB-sensitive parS-plasmid. The mutations obtained are widely distributed in the gene. Several of the mutations affected binding of ParB to parS; others did not. Amino acid substitutions that affected binding without influencing dimerization were mapped to two separate regions of ParB. C-Terminal amino acid substitutions in ParB blocked its dimerization and binding to parS, as did deletions of the entire C-terminal part of the protein. These results are consistent with ParB binding to parS as a dimer and suggest that the C-terminal part is a dimerization domain of the protein. Cell extracts of a frameshift mutant analyzed contained, in addition to the expected truncated ParB, a second species of ParB with the normal C-terminal part. Apparently, a site of ribosomal frameshifting is encoded within parB, at which some ribosomes change reading frame in the mutant. All obtained mutant ParB proteins were unable to complement the partition defect of a parB null mutant mini-P1. This suggests that the initial reactions between ParB and parS leading to partition dysfunction and to partition function are similar.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8676375 PubMed]<br /> Online version:[http://dx.doi.org/10.1006/jmbi.1996.0326 10.1006/jmbi.1996.0326]<br /> |-<br /> !align=left |Keywords<br /> ||<br /> Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophage P1/genetics; Base Sequence; Binding Sites; DNA Mutational Analysis; Genes, Reporter; Molecular Sequence Data; Plasmids/chemistry; Plasmids/genetics; Protein Conformation; Protein Denaturation; Sequence Homology, Amino Acid; Structure-Activity Relationship<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184753.J577db8e564d47&page=184753&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8676375&diff=1504159 PMID:8676375 2016-07-07T02:05:25Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8387444&diff=1504158 PMID:8387444 2016-07-07T02:05:25Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="O577db8e4a1921" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Dartois, V, De Backer, O and Colson, C''' (1993) Sequence of the Salmonella typhimurium StyLT1 restriction-modification genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence of helicase domains. ''Gene'' '''127''':105-10<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The StyLT1 restriction-modification (R-M) system of Salmonella typhimurium has recently been suggested to belong to the type-III R-M systems [De Backer and Colson, Gene 97 (1991) 103-107]. The nucleotide sequences of StyLT1 mod and res have been determined. Two closely adjacent open reading frames were found 12 bp apart with coding capacities of 651 (Mod) and 982 (Res) amino acids (aa), respectively. The genes, lying in the same direction of transcription in the mod-res order, are transcribed as distinct units. The deduced aa sequences reveal homologies with known type-III enzymes from the Escherichia coli P1 prophage, E. coli P15 plasmid and Bacillus cereus chromosome. In addition, the StyLT1 restriction endonuclease (ENase), like other type-I and type-III ENases, contains sequence motifs characteristic of superfamily-II helicases, which may be involved in DNA unwinding at the cleavage site.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8387444 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Amino Acid Sequence; Base Sequence; Conserved Sequence; DNA Helicases/genetics; DNA Helicases/metabolism; DNA, Bacterial; Deoxyribonucleases, Type III Site-Specific/genetics; Deoxyribonucleases, Type III Site-Specific/metabolism; Methyltransferases; Molecular Sequence Data; Salmonella typhimurium/enzymology; Salmonella typhimurium/genetics; Sequence Homology, Amino Acid; Site-Specific DNA-Methyltransferase (Adenine-Specific)/genetics; Site-Specific DNA-Methyltransferase (Adenine-Specific)/metabolism<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184752.O577db8e4a1921&page=184752&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:2211715&diff=1504157 PMID:2211715 2016-07-07T02:05:24Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="F577db8e4a184c" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Velleman, M, Heirich, M, Günther, A and Schuster, H''' (1990) A bacteriophage P1-encoded modulator protein affects the P1 c1 repression system. ''J. Biol. Chem.'' '''265''':18511-7<br /> |-<br /> !align=left |Abstract<br /> ||<br /> Bacteriophage P1 encodes a tripartite immunity system composed of the immC, immI, and immT region. Their basic genetic elements are the c1 repressor of lytic functions, the c4 repressor which negatively regulates antirepressor synthesis, and the bof gene, respectively. The function of the latter will be described here. We have cloned and sequenced the bof gene from P1 wild type and a P1 bof amber mutant. Based on the position of a TAG codon of the bof amber mutant the bof wild type gene was localized. It starts with a TTG codon, comprises 82 codons, and is preceded by a promoter structure. The bof protein (Mr = 7500) was overproduced in Escherichia coli from a bof recombinant plasmid and was purified to near homogeneity. The N-terminal amino acids predicted from the DNA sequence of the bof gene were confirmed by sequence analysis of the bof protein. Using a DNA mobility shift assay, we show that bof protein enhances the binding of c1 repressor to the operator of the c1 gene. In accordance with this result, in transformants of Escherichia coli, containing both a bof- and a c1-encoding plasmid, c1 expression is down-regulated. We conclude that bof acts as a modulator protein in the repression of a multitude of c1-controlled operators in the P1 genome.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2211715 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Base Sequence; Cloning, Molecular; Coliphages/genetics; Gene Expression Regulation, Viral; Genes, Viral; Molecular Sequence Data; Molecular Weight; Operator Regions, Genetic; Protein Binding; Recombinant Proteins; Regulatory Sequences, Nucleic Acid; Repressor Proteins/physiology; Restriction Mapping; Viral Proteins/genetics; Viral Proteins/isolation & purification; Viral Structural Proteins/genetics<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184751.F577db8e4a184c&page=184751&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8387444&diff=1504156 PMID:8387444 2016-07-07T02:05:24Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:2211715&diff=1504155 PMID:2211715 2016-07-07T02:05:24Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:2120849&diff=1504154 PMID:2120849 2016-07-07T02:05:24Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="A577db8e408850" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Baumstark, BR, Stovall, SR and Bralley, P''' (1990) The ImmC region of phage P1 codes for a gene whose product promotes lytic growth. ''Virology'' '''179''':217-27<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The ImmC region of the temperate bacteriophage P1 contains c1, a gene that codes for a repressor of lytic growth. Located in the region upstream of c1 are four open reading frames capable of coding for low-molecular-weight proteins. The efficiency of lysogeny by P1+Cm was found to be reduced by almost 10(5)-fold when the host cells carry this region of ImmC on a multicopy plasmid. The sequences responsible for interfering with lysogen formation were localized to one of the small open reading frames (orf4) within ImmC. Insertions and deletions within orf4 suppress the virulent phenotype of P1virC mutants when introduced into the phage by recombination. These virC-suppressed mutant phage were found to be incapable of lytic growth unless the product of orf4 is provided in trans. The presence of orf4 was observed to interfere with repression by the c1 protein of ImmC-encoded promoters fused to lacZ. For this reason, we suggest that orf4 corresponds to coi, a gene previously proposed to code for an inactivator of c1-mediated repression.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2120849 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Amino Acid Sequence; Base Sequence; Chromosome Deletion; Coliphages/genetics; Coliphages/growth & development; Escherichia coli/genetics; Genes, Viral; Genetic Complementation Test; Lysogeny; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligonucleotide Probes; Open Reading Frames; Plasmids; Transcription, Genetic; beta-Galactosidase/genetics; beta-Galactosidase/metabolism<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184749.A577db8e408850&page=184749&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8051007&diff=1504153 PMID:8051007 2016-07-07T02:05:24Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="B577db8e4086ef" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Heinrich, J, Citron, M, Günther, A and Schuster, H''' (1994) Second-site suppressors of the bacteriophage P1 virs mutant reveal the interdependence of the c4, icd, and ant genes in the P1 immI operon. ''J. Bacteriol.'' '''176''':4931-6<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The immI operon of phage P1 contains the genes c4, icd, and ant, which are transcribed in that order from the same constitutive promoter, P51b. The gene c4 encodes an antisense RNA which inhibits the synthesis of an antirepressor by acting on a target ant mRNA. Interaction depends on the complementarity of two pairs of short sequences encompassing virs+ and the ribosome-binding site involved in ant expression. Accordingly, in a P1 virs mutant phage, antirepressor is synthesized constitutively. We have isolated lysogen-proficient, second-site suppressors of P1 virs in order to evaluate the interdependence of the immI-specific genes. From a total of 17 suppressors analyzed, 15 were found to be located in the icd gene. They were identified as frameshift mutations, containing base insertions or deletions in tandem repeats of a single base pair. One suppressor was identified as a P51b promoter-down mutation; the second site of another suppressor was found to be located in the c4 gene. Furthermore, it was shown that virs cannot be suppressed by ant (icd+) suppressors. The results confirm the model that the immI operon is transcribed as a unit, that the icd and ant genes are translationally coupled, and that the constitutive synthesis of Icd protein alone is lethal to the bacterial cell. The existence of a c4 suppressor of virs, whose effect is not yet known, points to a still more complex regulation of antirepressor synthesis than was anticipated from the model.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8051007 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC196329 PMC196329]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Bacteriophage P1/genetics; Bacteriophage P1/pathogenicity; Base Sequence; DNA, Bacterial/genetics; Gene Expression Regulation, Viral; Genes, Suppressor; Genes, Viral; Molecular Sequence Data; Restriction Mapping; Viral Structural Proteins/genetics<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184750.B577db8e4086ef&page=184750&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:8051007&diff=1504152 PMID:8051007 2016-07-07T02:05:24Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:2120849&diff=1504151 PMID:2120849 2016-07-07T02:05:23Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7932755&diff=1504150 PMID:7932755 2016-07-07T02:05:21Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="V577db8e17ce87" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Skorupski, K, Sauer, B and Sternberg, N''' (1994) Faithful cleavage of the P1 packaging site (pac) requires two phage proteins, PacA and PacB, and two Escherichia coli proteins, IHF and HU. ''J. Mol. Biol.'' '''243''':268-82<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The PacA and PacB subunits of the bacteriophage P1 DNA packaging enzyme (pacase) are necessary for cleavage of the phage packaging site (pac). In the accompanying paper, we show that the PacA subunit of the enzyme specifically binds to pac in the absence of PacB, but requires factors present in an Escherichia coli extract to do so. We show here that either of two E. coli DNA binding proteins, integration host factor (IHF) or HU, can replace this extract and promote the binding of PacA to pac. IHF binds to pac independently of PacA and DNase I footprinting experiments show that IHF protects approximately 40 bp of DNA around an IHF consensus sequence adjacent to the cleavage site. DNase I footprinting experiments also show that in the presence of either IHF or HU, PacA binds to the hexanucleotide sequences (5'-TGATCA/G) that flank the cleavage site and that have been previously shown to be essential for pac cleavage. The importance of IHF and HU in pac cleavage is further demonstrated by the severe reduction in both the fidelity and efficiency of pac cleavage in vitro with extracts lacking both IHF and HU. Addition of either IHF or HU to the deficient extracts renders them fully proficient for pac cleavage. Finally, we show that IHF bends DNA at the IHF site within pac. Based on these results, we propose a model that can account for the role of the various phage and host proteins, and for DNA bending in the pac cleavage reaction.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7932755 PubMed]<br /> Online version:[http://dx.doi.org/10.1006/jmbi.1994.1653 10.1006/jmbi.1994.1653]<br /> |-<br /> !align=left |Keywords<br /> ||<br /> Bacterial Proteins/metabolism; Bacteriophage P1/genetics; Bacteriophage P1/metabolism; Base Sequence; Binding Sites; DNA, Viral/metabolism; DNA-Binding Proteins/metabolism; Endodeoxyribonucleases; Escherichia coli/metabolism; Escherichia coli/virology; Integration Host Factors; Models, Theoretical; Molecular Sequence Data; Nucleic Acid Conformation; Viral Proteins/metabolism<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184748.V577db8e17ce87&page=184748&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7932755&diff=1504149 PMID:7932755 2016-07-07T02:05:21Z

<p>5.9.72.48: New PMID: Page!</p> <hr /> <div>PMID on Demand placeholder</div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7932754&diff=1504148 PMID:7932754 2016-07-07T02:05:21Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="S577db8e0d998c" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Skorupski, K, Sternberg, N and Sauer, B''' (1994) Purification and DNA-binding activity of the PacA subunit of the bacteriophage P1 pacase enzyme. ''J. Mol. Biol.'' '''243''':258-67<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The bacteriophage P1 packaging site (pac) cleavage enzyme (pacase) consists of two phage encoded proteins, PacA and PacB. Both proteins are necessary for the recognition and cleavage of pac and for subsequent packaging of cleaved DNA into phage particles. We have purified PacA to homogeneity from a bacterial strain that overproduces the protein. Purified PacA complements an Escherichia coli extract containing the PacB protein for DNA cleavage at the pac site and recognizes and binds to methylated pac DNA independently of PacB in gel retardation experiments. The latter property of PacA is absolutely dependent on the presence of a wildtype E. coli extract, suggesting that E. coli host proteins play a role in the pac cleavage reaction.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7932754 PubMed]<br /> Online version:[http://dx.doi.org/10.1006/jmbi.1994.1652 10.1006/jmbi.1994.1652]<br /> |-<br /> !align=left |Keywords<br /> ||<br /> Bacterial Proteins/metabolism; Bacteriophage P1/enzymology; Bacteriophage P1/genetics; Base Sequence; Chromatography, Liquid; Cloning, Molecular; DNA, Viral/metabolism; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/metabolism; Endodeoxyribonucleases; Escherichia coli/metabolism; Molecular Sequence Data; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Viral Proteins/genetics; Viral Proteins/isolation & purification; Viral Proteins/metabolism<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184747.S577db8e0d998c&page=184747&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7932754&diff=1504147 PMID:7932754 2016-07-07T02:05:20Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7597035&diff=1504146 PMID:7597035 2016-07-07T02:05:20Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="D577db8e0410cd" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Hartmann, RK, Heinrich, J, Schlegl, J and Schuster, H''' (1995) Precursor of C4 antisense RNA of bacteriophages P1 and P7 is a substrate for RNase P of Escherichia coli. ''Proc. Natl. Acad. Sci. U.S.A.'' '''92''':5822-6<br /> |-<br /> !align=left |Abstract<br /> ||<br /> The C4 repressor of the temperate bacteriophages P1 and P7 inhibits antirepressor (Ant) synthesis and is essential for establishment and maintenance of lysogeny. C4 is an antisense RNA acting on a target, Ant mRNA, which is transcribed from the same promoter. The antisense-target RNA interaction requires processing of C4 RNA from a precursor RNA. Here we show that 5' maturation of C4 RNA in vivo depends on RNase P. In vitro, Escherichia coli RNase P and its catalytic RNA subunit (M1 RNA) can generate the mature 5' end of C4 RNA from P1 by a single endonucleolytic cut, whereas RNase P from the E. coli rnpA49 mutant, carrying a missense mutation in the RNase P protein subunit, is defective in the 5' maturation of C4 RNA. Primer extension analysis of RNA transcribed in vivo from a plasmid carrying the P1 c4 gene revealed that 5'-mature C4 RNA was the predominant species in rnpA+ bacteria, whereas virtually no mature C4 RNA was found in the temperature-sensitive rnpA49 strain at the restrictive temperature. Instead, C4 RNA molecules carrying up to five extra nucleotides beyond the 5' end accumulated. The same phenotype was observed in rnpA+ bacteria which harbored a plasmid carrying a P7 c4 mutant gene with a single C-->G base substitution in the structural homologue to the CCA 3' end of tRNAs. Implications of C4 RNA processing for the lysis/lysogeny decision process of bacteriophages P1 and P7 are discussed.<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7597035 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC41593 PMC41593]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Bacteriophage P1/genetics; Bacteriophage P1/metabolism; Base Sequence; Coliphages/genetics; Coliphages/metabolism; DNA Primers; Endoribonucleases/isolation & purification; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Genes, Bacterial; Genes, Fungal; Molecular Sequence Data; Nucleic Acid Conformation; Polymerase Chain Reaction; RNA Precursors/metabolism; RNA, Antisense/biosynthesis; RNA, Antisense/chemistry; RNA, Catalytic/isolation & purification; RNA, Catalytic/metabolism; RNA, Messenger/biosynthesis; RNA, Transfer, Gly/biosynthesis; RNA, Transfer, Gly/isolation & purification; RNA, Viral/biosynthesis; RNA, Viral/chemistry; Repressor Proteins/biosynthesis; Ribonuclease P; Transcription, Genetic<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184746.D577db8e0410cd&page=184746&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7597035&diff=1504145 PMID:7597035 2016-07-07T02:05:20Z

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5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7330064&diff=1504144 PMID:7330064 2016-07-07T02:05:19Z

<p>5.9.72.48: Fill PMID: Page!</p> <hr /> <div>{{RightTOC}}<br /> <br /> <br /> {| id="D577db8df98e64" class=" tableEdit PMID_info_table" <br /> <br /> |-<br /> !align=left |Citation<br /> ||<br /> '''Walker, JT and Walker, DH Jr''' (1981) Structural proteins of coliphage P1. ''Prog. Clin. Biol. Res.'' '''64''':69-77<br /> |-<br /> !align=left |Abstract<br /> ||<br /> No abstract in PubMed<br /> |-<br /> !align=left |Links<br /> ||<br /> [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7330064 PubMed]<br /> <br /> |-<br /> !align=left |Keywords<br /> ||<br /> Coliphages/genetics; Coliphages/ultrastructure; Electrophoresis, Polyacrylamide Gel; Genes, Viral; Molecular Weight; Morphogenesis; Viral Proteins/analysis; Viral Proteins/genetics; Virus Replication<br /> <br /> |- class="tableEdit_footer" <br /> |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.184745.D577db8df98e64&page=184745&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||<br /> |}<br /> <br /> <br /> ==Significance {{HelpIcon|Help:Literature}} ==<br /> {{LitSignificance}}<br /> <br /> == Useful Materials and Methods {{HelpIcon|Help:Literature}}==<br /> {{LitMaterials}}<br /> <br /> ==Annotations {{HelpIcon|Help:Literature}}==<br /> <annotationlinks/><br /> <br /> ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==<br /> {{LitLinks}}<br /> <br /> ==See also==<br /> <br /> ==References==<br /> {{RefHelp}}<br /> <references/></div>

5.9.72.48 https://ecoliwiki.org/colipedia/index.php?title=PMID:7330064&diff=1504143 PMID:7330064 2016-07-07T02:05:19Z

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5.9.72.48