EcoliWiki - User contributions [en]

Category:GO:0031230 ! intrinsic to cell outer membrane

2008-08-20T21:05:26Z

64.191.81.117: New GO term category page

Category:GO:0009970 ! cellular response to sulfate starvation

2008-08-20T20:26:52Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0009970_!_cellular_response_to_sulfate_starvation}}

Category:GO:0008703 ! 5-amino-6-(5-phosphoribosylamino)uracil reductase activity

2008-08-20T20:26:14Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0008703_!_5-amino-6-(5-phosphoribosylamino)uracil_reductase_activity}}

PMID:16236133

2008-08-20T20:04:20Z

64.191.81.117: Fill PMID: Page!

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 '''Odsbu, I, Klungsøyr, HK, Fossum, S and Skarstad, K''' (2005) Specific N-terminal interactions of the Escherichia coli SeqA protein are required to form multimers that restrain negative supercoils and form foci.''Genes Cells'' '''10''':1039-49

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The Escherichia coli SeqA protein binds preferentially to hemimethylated DNA and is required for inactivation (sequestration) of newly formed origins. A mutant SeqA protein, SeqA4 (A25T), which is deficient in origin sequestration in vivo, was found here to have lost the ability to form multimers, but could bind as dimers with wild-type affinity to a pair of hemimethylated GATC sites. In vitro, binding of SeqA dimers to a plasmid first generates a topology change equivalent to a few positive supercoils, then the binding leads to a topology change in the "opposite" direction, resulting in a restraint of negative supercoils. Binding of SeqA4 mutant dimers produced the former effect, but not the latter, showing that a topology change equivalent to positive supercoiling is caused by the binding of single dimers, whereas restraint of negative supercoils requires multimerization via the N-terminus. In vivo, mutant SeqA4 protein was not capable of forming foci observed by immunofluorescence microscopy, showing that N-terminus-dependent multimerization is required for building SeqA foci. Overproduction of SeqA4 led to partially restored initiation synchrony, indicating that origin sequestration may not depend on efficient higher-order multimerization into foci, but do require a high local concentration of SeqA.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16236133 PubMed] Online version:[http://dx.doi.org/10.1111/j.1365-2443.2005.00898.x 10.1111/j.1365-2443.2005.00898.x]
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{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:16236133

2008-08-20T20:04:20Z

64.191.81.117: New PMID: Page!

Category:GO:0010124 ! phenylacetate catabolic process

2008-08-20T19:58:53Z

64.191.81.117: New GO term category page

Category:GO:0006413 ! translational initiation

2008-08-20T19:56:26Z

64.191.81.117: New GO term category page

Category:GO:0043022 ! ribosome binding

2008-08-20T19:56:25Z

64.191.81.117: New GO term category page

PMID:6445562

2008-08-20T18:47:44Z

64.191.81.117: Fill PMID: Page!

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 '''Yates, JL, Arfsten, AE and Nomura, M''' (1980) In vitro expression of Escherichia coli ribosomal protein genes: autogenous inhibition of translation.''Proc. Natl. Acad. Sci. U.S.A.'' '''77''':1837-41

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Escherichia coli ribosomal protein L1 (0.5 micro M) was found to inhibit the synthesis of both proteins of the L11 operon, L11 and L1, but not the synthesis of other proteins directed by lambda rifd 18 DNA. Similarly, S4 (1 micro M) selectively inhibited the synthesis of three proteins of the alpha operon, S13, S11, and S4, directed by lambda spcI DNA or a restriction enzyme fragment obtained from this DNA. S8 (3.6 micro M) also showed preferential inhibitory effects on the synthesis of some proteins encoded in the spc operon, L24 and L5 (and probably S14 and S8), directed by lambda spcl DNA or a restriction enzyme fragment carrying the genes for these proteins. The inhibitory effect of L1 was observed only with L1 and not with other proteins examined, including S4 and S8. Similarly, the effect of S4 was not observed with L1 or S8, and that of S8 was not seen with L1 or S4. Inhibition was shown to take place at the level of translation rather than transcription. Thus, at least some ribosomal proteins (L1 S4, and S8) have the ability to cause selective translational inhibition of the synthesis of certain ribosomal proteins whose genes are in the same operon as their own. These results support the hypothesis that certain free ribosomal proteins not assembled into ribosomes act as "autogenous" feedback inhibitors to regulate the synthesis of ribosomal proteins.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6445562 PubMed] 
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<protect>

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.136286.O48ac66d03a737&page=136286&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:6445562

2008-08-20T18:47:44Z

64.191.81.117: New PMID: Page!

Category:GO:0022627 ! cytosolic small ribosomal subunit

2008-08-20T18:46:44Z

64.191.81.117: New GO term category page

PMID:10852867

2008-08-20T18:42:15Z

64.191.81.117: Fill PMID: Page!

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 '''Matsumoto, G, Homma, T, Mori, H and Ito, K''' (2000) A mutation in secY that causes enhanced SecA insertion and impaired late functions in protein translocation.''J. Bacteriol.'' '''182''':3377-82

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|{{TableHeadingColor}} |'''Abstract''' || <protect>A cold-sensitive secY mutant (secY125) with an amino acid substitution in the first periplasmic domain causes in vivo retardation of protein export. Inverted membrane vesicles prepared from this mutant were as active as the wild-type membrane vesicles in translocation of a minute amount of radioactive preprotein. The mutant membrane also allowed enhanced insertion of SecA, and this SecA insertion was dependent on the SecD and SecF functions. These and other observations suggested that the early events in translocation, such as SecA-dependent insertion of the signal sequence region, is actually enhanced by the SecY125 alteration. In contrast, since the mutant membrane vesicles had decreased capacity to translocate chemical quantity of pro-OmpA and since they were readily inactivated by pretreatment of the vesicles under the conditions in which a pro-OmpA translocation intermediate once accumulated, the late translocation functions appear to be impaired. We conclude that this periplasmic secY mutation causes unbalanced early and late functions in translocation, compromising the translocase's ability to catalyze multiple rounds of reactions.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10852867 PubMed] 
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<protect>

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.136284.S48ac65879f920&page=136284&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:10852867

2008-08-20T18:42:15Z

64.191.81.117: New PMID: Page!

PMID:8190079

2008-08-20T18:41:55Z

64.191.81.117: Fill PMID: Page!

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 '''Taura, T, Akiyama, Y and Ito, K''' (1994) Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes.''Mol. Gen. Genet.'' '''243''':261-9

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|{{TableHeadingColor}} |'''Abstract''' || <protect>A number of secY mutants of Escherichia coli showing protein export defects were isolated by a combination of localized mutagenesis and secA-lacZ screening. Most of them were cold sensitive and contained single base substitutions in secY leading to amino acid replacements in various parts of the SecY protein, mainly in the cytoplasmic and the transmembrane domains. A temperature-sensitive mutant with an export defect had the same base substitution as secY24, which was characterized previously. Many cold-sensitive secY mutants exhibited rapid responses to temperature lowering but their apparent defects varied at the permissive temperature. Others exhibited delayed responses to the temperature shift. Some secY mutations, including secY39, interfered with protein export when expressed from a multicopy plasmid, even in the presence of wild-type secY on the chromosome. Such "dominant negative" mutations, including secY-d1, which was studied previously, were all located in either cytoplasmic domain 5 or 6, which is consistent with our previous proposal that the C-terminal region of SecY is important for its function as a protein translocator. We also studied the phenotypes of strains in which one of the secY mutations was combined with the components of the secD operon. Overexpression of secD partially suppressed the secY39 mutation, while overexpression of secF exacerbated the export defects of secY122 and secY125 mutations. Overexpression of "yajC", located within the secD operon, suppressed secY-d1. Although yajC itself proved to be dispensable, its disruption impaired the growth of the secY39 mutant at 42 degrees C. These observations suggest that SecY interacts with SecD, SecF, and the product of yajC.</protect>
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8190079 PubMed] 
|}

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<protect>

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.136283.P48ac657394a71&page=136283&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:8190079

2008-08-20T18:41:55Z

64.191.81.117: New PMID: Page!

Category:GO:0032977 ! membrane insertase activity

2008-08-20T18:25:07Z

64.191.81.117: New GO term category page

Category:GO:0016020 ! membrane

2008-08-20T18:24:50Z

64.191.81.117: New GO term category page

Category:GO:0051205 ! protein insertion into membrane

2008-08-20T18:24:36Z

64.191.81.117: New GO term category page

Category:GO:0030170 ! pyridoxal phosphate binding

2008-08-20T18:24:17Z

64.191.81.117: New GO term category page

Category:GO:0050790 ! regulation of catalytic activity

2008-08-20T18:19:43Z

64.191.81.117: New GO term category page

Category:GO:0019899 ! enzyme binding

2008-08-20T18:16:59Z

64.191.81.117: New GO term category page

Category:GO:0006402 ! mRNA catabolic process

2008-08-20T18:16:34Z

64.191.81.117: New GO term category page

Category:GO:0008428 ! ribonuclease inhibitor activity

2008-08-20T18:15:56Z

64.191.81.117: New GO term category page

Category:GO:0006749 ! glutathione metabolic process

2008-08-20T17:21:09Z

64.191.81.117: New GO term category page

Category:GO:0009109 ! coenzyme catabolic process

2008-08-20T17:20:35Z

64.191.81.117: New GO term category page

Category:GO:0044248 ! cellular catabolic process

2008-08-20T17:20:08Z

64.191.81.117: New GO term category page

Category:GO:0008238 ! exopeptidase activity

2008-08-20T17:19:52Z

64.191.81.117: New GO term category page

Category:GO:0004175 ! endopeptidase activity

2008-08-20T16:31:57Z

64.191.81.117: New GO term category page

Category:GO:0042273 ! ribosomal large subunit biogenesis and assembly

2008-08-20T15:21:55Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0042273_!_ribosomal_large_subunit_biogenesis_and_assembly}}

Category:GO:0004826 ! phenylalanine-tRNA ligase activity

2008-08-20T15:09:36Z

64.191.81.117: New GO term category page

Category:GO:0006432 ! phenylalanyl-tRNA aminoacylation

2008-08-20T15:09:25Z

64.191.81.117: New GO term category page

Category:GO:0004829 ! threonine-tRNA ligase activity

2008-08-20T15:00:16Z

64.191.81.117: New GO term category page

Category:GO:0006435 ! threonyl-tRNA aminoacylation

2008-08-20T15:00:01Z

64.191.81.117: New GO term category page

Category:GO:0042256 ! mature ribosome assembly

2008-08-20T14:56:55Z

64.191.81.117: New GO term category page

Category:GO:0003743 ! translation initiation factor activity

2008-08-20T14:56:20Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0003743_!_translation_initiation_factor_activity}}

Category:GO:0009605 ! response to external stimulus

2008-08-20T14:35:30Z

64.191.81.117: New GO term category page

Category:GO:0009991 ! response to extracellular stimulus

2008-08-20T14:34:48Z

64.191.81.117: New GO term category page

Category:GO:0031119 ! tRNA pseudouridine synthesis

2008-08-20T14:12:14Z

64.191.81.117: New GO term category page

Category:GO:0016439 ! tRNA-pseudouridine synthase activity

2008-08-20T14:12:01Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0016439_!_tRNA-pseudouridine_synthase_activity}}

Category:GO:0016434 ! rRNA (cytosine) methyltransferase activity

2008-08-20T13:20:34Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0016434_!_rRNA_(cytosine)_methyltransferase_activity}}

Category:GO:0003911 ! DNA ligase (NAD ) activity

2008-08-20T13:01:20Z

64.191.81.117: New GO term category page

Category:GO:0006928 ! cell motility

2008-08-20T11:53:17Z

64.191.81.117: New GO term category page

Category:GO:0004614 ! phosphoglucomutase activity

2008-08-20T09:04:39Z

64.191.81.117: New GO term category page

Category:GO:0016868 ! intramolecular transferase activity, phosphotransferases

2008-08-20T09:04:26Z

64.191.81.117: New GO term category page

{{GO term stub|GO:0016868_!_intramolecular_transferase_activity,_phosphotransferases}}

Category:GO:0005998 ! xylulose catabolic process

2008-08-20T08:48:06Z

64.191.81.117: New GO term category page

Category:GO:0009045 ! xylose isomerase activity

2008-08-20T08:46:59Z

64.191.81.117: New GO term category page

Category:GO:0009030 ! thiamin phosphate kinase activity

2008-08-20T07:58:57Z

64.191.81.117: New GO term category page

Category:GO:0018364 ! peptidyl-glutamine methylation

2008-08-20T07:27:48Z

64.191.81.117: New GO term category page

Category:GO:0008276 ! protein methyltransferase activity

2008-08-20T07:27:31Z

64.191.81.117: New GO term category page

Category:GO:0051454 ! intracellular pH elevation

2008-08-20T06:26:19Z

64.191.81.117: New GO term category page