EcoliWiki - User contributions [en]

Category:GO:0004801 ! sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

2012-02-26T16:11:18Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004801_!_sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate_glyceronetransferase_activity}}

==References==
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PMID:2864330

2012-02-26T14:05:28Z

38.101.148.126: Fill PMID: Page!

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{| id="B4f4a3c270ee73" class=" tableEdit PMID_info_table"

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!align=left |Citation
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'''Kölling, R and Lother, H''' (1985) AsnC: an autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli.''J. Bacteriol.'' '''164''':310-5
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!align=left |Abstract
||
The regulation of the asparagine synthetase A gene of Escherichia coli was studied in vitro with a coupled transcription-translation system. It was shown that the 17-kilodalton gene, which is transcribed divergently from the adjacent asnA gene, codes for an activator of asnA transcription. The synthesis of the 17-kilodalton protein, which we now call AsnC, is autogenously regulated. The stimulating effect of AsnC on asnA transcription is abolished by asparagine, while the autoregulation of asnC is not affected by asparagine. The N-terminal part of the asnC protein, inferred from the DNA sequence, is homologous to the DNA-binding domain of regulatory proteins like catabolite gene activator, cro, and cI. This homology and direct repeats found in the region of the two asn promoters suggest that the asnC protein regulates transcription by binding to DNA. The asn promoters were defined by mapping of the mRNA start sites of in vitro-generated transcripts.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2864330 PubMed]

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!align=left |Keywords
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Asparagine; Aspartate-Ammonia Ligase; Base Sequence; DNA-Binding Proteins; Escherichia coli; Gene Expression Regulation; Genes, Regulator; Ligases; Promoter Regions, Genetic; Transcription, Genetic

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<protect>

{| id="E4f4a3c28a8da9" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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==References==
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PMID:2864330

2012-02-26T14:05:26Z

38.101.148.126: New PMID: Page!

Category:GO:0006007 ! glucose catabolic process

2012-02-25T11:19:26Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0006007_!_glucose_catabolic_process}}

==References==
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Category:GO:0004523 ! ribonuclease H activity

2012-02-25T10:29:53Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004523_!_ribonuclease_H_activity}}

==References==
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Category:GO:0004825 ! methionine-tRNA ligase activity

2012-02-24T21:38:54Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004825_!_methionine-tRNA_ligase_activity}}

==References==
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<references/>

PMID:2211496

2012-02-24T19:41:10Z

38.101.148.126: Fill PMID: Page!

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{| id="H4f47e7d5d4968" class=" tableEdit PMID_info_table"

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!align=left |Citation
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'''Guthrie, B and Wickner, W''' (1990) Trigger factor depletion or overproduction causes defective cell division but does not block protein export.''J. Bacteriol.'' '''172''':5555-62
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!align=left |Abstract
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Trigger factor is an abundant cytosolic protein of Escherichia coli which can stabilize proOmpA for in vitro translocation across inner membrane vesicles. The gene encoding E. coli trigger factor was isolated and sequenced, allowing construction of strains in which the expression of trigger factor is readily regulated. We found no defect in the in vivo rate of synthesis or secretion of proOmpA in trigger factor-depleted cells. The primary physiological defect in trigger factor-depleted or -overproducing cells is an enrichment of filamented cells. Filamentation of the trigger factor-overproducing strain is suppressed by a multicopy plasmid expressing the essential division gene ftsZ, suggesting that trigger factor has an important role in cell division.
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!align=left |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2211496 PubMed]

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!align=left |Keywords
||
Amino Acid Isomerases; Amino Acid Sequence; Bacterial Outer Membrane Proteins; Bacterial Proteins; Base Sequence; Carrier Proteins; Cell Division; Chromosome Deletion; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Gene Library; Genes, Bacterial; Molecular Sequence Data; Mutation; Oligonucleotide Probes; Peptidylprolyl Isomerase; Protein Precursors; Restriction Mapping

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{| id="T4f47e7d5e7ba0" class=" tableEdit GO_table_reference dataTable"
|- {{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=d41d8cd98f00b204e9800998ecf8427e.180964.T4f47e7d5e7ba0&page=180964&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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==References==
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PMID:2211496

2012-02-24T19:41:09Z

38.101.148.126: New PMID: Page!

Category:GO:0009113 ! purine base biosynthetic process

2012-02-23T20:33:33Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0009113_!_purine_base_biosynthetic_process}}

==References==
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Category:GO:0015693 ! magnesium ion transport

2012-02-23T00:16:03Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0015693_!_magnesium_ion_transport}}

==References==
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Category:GO:0003724 ! RNA helicase activity

2012-02-22T19:56:33Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0003724_!_RNA_helicase_activity}}

==References==
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Category:GO:0016832 ! aldehyde-lyase activity

2012-02-22T11:43:18Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0016832_!_aldehyde-lyase_activity}}

==References==
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Category:GO:0004527 ! exonuclease activity

2012-02-22T09:36:17Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004527_!_exonuclease_activity}}

==References==
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Category:GO:0003848 ! 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity

2012-02-22T08:53:59Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0003848_!_2-amino-4-hydroxy-6-hydroxymethyldihydropteridine_diphosphokinase_activity}}

==References==
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PMID:16385024

2012-02-22T05:38:45Z

38.101.148.126: Fill PMID: Page!

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<protect>
 '''Sanchez, H, Kidane, D, Castillo Cozar, M, Graumann, PL and Alonso, JC''' (2006) Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the absence of DNA end processing.''J. Bacteriol.'' '''188''':353-60

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The recognition and processing of double-strand breaks (DSBs) to a 3' single-stranded DNA (ssDNA) overhang structure in Bacillus subtilis is poorly understood. Mutations in addA and addB or null mutations in recJ (DeltarecJ), recQ (DeltarecQ), or recS (DeltarecS) genes, when present in otherwise-Rec+ cells, render cells moderately sensitive to the killing action of different DNA-damaging agents. Inactivation of a RecQ-like helicase (DeltarecQ or DeltarecS) in addAB cells showed an additive effect; however, when DeltarecJ was combined with addAB, a strong synergistic effect was observed with a survival rate similar to that of DeltarecA cells. RecF was nonepistatic with RecJ or AddAB. After induction of DSBs, RecN-yellow fluorescent protein (YFP) foci were formed in addAB DeltarecJ cells. AddAB and RecJ were required for the formation of a single RecN focus, because in their absence multiple RecN-YFP foci accumulated within the cells. Green fluorescent protein-RecA failed to form filamentous structures (termed threads) in addAB DeltarecJ cells. We propose that RecN is one of the first recombination proteins detected as a discrete focus in live cells in response to DSBs and that either AddAB or RecQ(S)-RecJ are required for the generation of a duplex with a 3'-ssDNA tail needed for filament formation of RecA.</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=16385024 PubMed]
Online version:[http://dx.doi.org/10.1128/JB.188.2.353-360.2006 10.1128/JB.188.2.353-360.2006]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
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<protect>

{| id="H4f447f658c0ce" class=" tableEdit GO_table_reference dataTable"
|- {{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=d41d8cd98f00b204e9800998ecf8427e.180950.H4f447f658c0ce&page=180950&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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==References==
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PMID:16385024

2012-02-22T05:38:45Z

38.101.148.126: New PMID: Page!

Category:GO:0003906 ! DNA-(apurinic or apyrimidinic site) lyase activity

2012-02-22T05:15:23Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0003906_!_DNA-(apurinic_or_apyrimidinic_site)_lyase_activity}}

==References==
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Category:GO:0006531 ! aspartate metabolic process

2012-02-22T05:11:23Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0006531_!_aspartate_metabolic_process}}

==References==
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Category:GO:0009291 ! unidirectional conjugation

2012-02-22T05:03:22Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0009291_!_unidirectional_conjugation}}

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PMID:16460018

2012-02-22T00:46:47Z

38.101.148.126: Fill PMID: Page!

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<protect>
 '''Bilder, P, Lightle, S, Bainbridge, G, Ohren, J, Finzel, B, Sun, F, Holley, S, Al-Kassim, L, Spessard, C, Melnick, M, Newcomer, M and Waldrop, GL''' (2006) The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.''Biochemistry'' '''45''':1712-22

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|{{TableHeadingColor}} |'''Abstract''' || <protect>Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterial carboxyltransferase (CT) subunit of ACC is a target for the design of novel therapeutics that combat severe, hospital-acquired infections resistant to the established classes of frontline antimicrobials. Here, we present the structures of the bacterial CT subunits from two prevalent nosocomial pathogens, Staphylococcus aureus and Escherichia coli, at a resolution of 2.0 and 3.0 A, respectively. Both structures reveal a small, independent zinc-binding domain that lacks a complement in the primary sequence or structure of the eukaryotic homologue.</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=16460018 PubMed]
Online version:[http://dx.doi.org/10.1021/bi0520479 10.1021/bi0520479]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitMaterials}}

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<protect>

{| id="P4f443af7954bc" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.180944.P4f443af7954bc&page=180944&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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</protect>

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PMID:16460018

2012-02-22T00:46:47Z

38.101.148.126: New PMID: Page!

Category:GO:0047001 ! 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase activity

2012-02-21T20:59:16Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0047001_!_2-dehydro-3-deoxy-D-gluconate_5-dehydrogenase_activity}}

==References==
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PMID:1614242

2012-02-21T02:44:14Z

38.101.148.126: Fill PMID: Page!

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<protect>
 '''Ohman, JL''' (1992) Allergen immunotherapy. Review of efficacy and current practice.''Med. Clin. North Am.'' '''76''':977-91

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|{{TableHeadingColor}} |'''Abstract''' || <protect>The modern use of allergen immunotherapy is described. Evidence for efficacy in inhalant allergy and insect sting allergy is reviewed. Current indications for allergen immunotherapy are discussed.</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=1614242 PubMed]

|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
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<protect>

{| id="P4f4304fe3375b" class=" tableEdit GO_table_reference dataTable"
|- {{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=d41d8cd98f00b204e9800998ecf8427e.180939.P4f4304fe3375b&page=180939&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:1614242

2012-02-21T02:44:13Z

38.101.148.126: New PMID: Page!

Category:GO:0004298 ! threonine-type endopeptidase activity

2012-02-20T09:08:45Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004298_!_threonine-type_endopeptidase_activity}}

==References==
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Category:GO:0008202 ! steroid metabolic process

2012-02-20T02:48:34Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0008202_!_steroid_metabolic_process}}

==References==
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PMID:12826616

2012-02-19T16:49:22Z

38.101.148.126: Fill PMID: Page!

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<protect>
 '''Mello, BA and Tu, Y''' (2003) Quantitative modeling of sensitivity in bacterial chemotaxis: the role of coupling among different chemoreceptor species.''Proc. Natl. Acad. Sci. U.S.A.'' '''100''':8223-8

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|{{TableHeadingColor}} |'''Abstract''' || <protect>We propose a general theoretical framework for modeling receptor sensitivity in bacterial chemotaxis, taking into account receptor interactions, including those among different receptor species. We show that our model can quantitatively explain the recent in vivo measurements of receptor sensitivity at different ligand concentrations for both mutant and wild-type strains. For mutant strains, our model can fit the experimental data exactly. For the wild-type cell, our model is capable of achieving high gain while having modest values of Hill coefficient for the response curves. Furthermore, the high sensitivity of the wild-type cell in our model is maintained for a wide range of ambient ligand concentrations, facilitated by near-perfect adaptation and dependence of ligand binding on receptor activity. Our study reveals the importance of coupling among different chemoreceptor species, in particular strong interactions between the aspartate (Tar) and serine (Tsr) receptors, which is crucial in explaining both the mutant and wild-type data. Predictions for the sensitivity of other mutant strains and possible improvements of our model for the wild-type cell are also discussed.</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=12826616 PubMed]
Online version:[http://dx.doi.org/10.1073/pnas.1330839100 10.1073/pnas.1330839100]
|}
</protect>
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{| id="U4f4128124982f" class=" tableEdit GO_table_reference dataTable"
|- {{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=d41d8cd98f00b204e9800998ecf8427e.180935.U4f4128124982f&page=180935&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
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PMID:12826616

2012-02-19T16:49:21Z

38.101.148.126: New PMID: Page!

PMID:4921251

2012-02-19T11:26:58Z

38.101.148.126: Fill PMID: Page!

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<protect>
 '''Björk, GR and Isaksson, LA''' (1970) Isolation of mutants of Escherichia coli lac king 5-methyluracil in transfer ribonucleic acid or 1-methylguanine in ribosomal RNA.''J. Mol. Biol.'' '''51''':83-100

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|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</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=4921251 PubMed]

|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
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<protect>

{| id="R4f40dc8245629" class=" tableEdit GO_table_reference dataTable"
|- {{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=d41d8cd98f00b204e9800998ecf8427e.180934.R4f40dc8245629&page=180934&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
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==References==
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PMID:4921251

2012-02-19T11:26:55Z

38.101.148.126: New PMID: Page!

Category:GO:0008776 ! acetate kinase activity

2012-02-19T05:36:03Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0008776_!_acetate_kinase_activity}}

==References==
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Category:GO:0006302 ! double-strand break repair

2012-02-18T21:22:38Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0006302_!_double-strand_break_repair}}

==References==
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Category:GO:0004070 ! aspartate carbamoyltransferase activity

2012-02-18T19:02:21Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004070_!_aspartate_carbamoyltransferase_activity}}

==References==
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Category:GO:0046167 ! glycerol-3-phosphate biosynthetic process

2012-02-18T16:07:17Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0046167_!_glycerol-3-phosphate_biosynthetic_process}}

==References==
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Category:GO:0031554 ! regulation of transcription termination, DNA-dependent

2012-02-18T14:32:14Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0031554_!_regulation_of_transcription_termination,_DNA-dependent}}

==References==
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Category:GO:0008700 ! 4-hydroxy-2-oxoglutarate aldolase activity

2012-02-18T13:22:31Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0008700_!_4-hydroxy-2-oxoglutarate_aldolase_activity}}

==References==
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Category:GO:0004190 ! aspartic-type endopeptidase activity

2012-02-18T01:55:14Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004190_!_aspartic-type_endopeptidase_activity}}

==References==
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Category:GO:0006353 ! transcription termination, DNA-dependent

2012-02-18T01:39:36Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0006353_!_transcription_termination,_DNA-dependent}}

==References==
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Category:GO:0004427 ! inorganic diphosphatase activity

2012-02-17T10:41:30Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004427_!_inorganic_diphosphatase_activity}}

==References==
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PMID:2900236

2012-02-17T06:53:17Z

38.101.148.126: Fill PMID: Page!

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<protect>
 '''McCarn, DF, Whitaker, RA, Alam, J, Vrba, JM and Curtis, SE''' (1988) Genes encoding the alpha, gamma, delta, and four F0 subunits of ATP synthase constitute an operon in the cyanobacterium Anabaena sp. strain PCC 7120.''J. Bacteriol.'' '''170''':3448-58

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|{{TableHeadingColor}} |'''Abstract''' || <protect>A cluster of genes encoding subunits of ATP synthase of Anabaena sp. strain PCC 7120 was cloned, and the nucleotide sequences of the genes were determined. This cluster, denoted atp1, consists of four F0 genes and three F1 genes encoding the subunits a (atpI), c (atpH), b' (atpG), b (atpF), delta (atpD), alpha (aptA), and gamma (atpC) in that order. Closely linked upstream of the ATP synthase subunit genes is an open reading frame denoted gene 1, which is equivalent to the uncI gene of Escherichia coli. The atp1 gene cluster is at least 10 kilobase pairs distant in the genome from apt2, a cluster of genes encoding the beta (atpB) and epsilon (atpE) subunits of the ATP synthase. This two-clustered ATP synthase gene arrangement is intermediate between those found in chloroplasts and E. coli. A unique feature of the Anabaena atp1 cluster is overlap between the coding regions for atpF and atpD. The atp1 cluster is transcribed as a single 7-kilobase polycistronic mRNA that initiates 140 base pairs upstream of gene 1. The deduced translation products for the Anabaena sp. strain PCC 7120 subunit genes are more similar to chloroplast ATP synthase subunits than to those of E. coli.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2900236 PubMed]

|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{| id="P4f3df95d90cf6" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.180919.P4f3df95d90cf6&page=180919&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:2900236

2012-02-17T06:53:17Z

38.101.148.126: New PMID: Page!

Category:GO:0006352 ! transcription initiation, DNA-dependent

2012-02-16T15:57:38Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0006352_!_transcription_initiation,_DNA-dependent}}

==References==
{{RefHelp}}
<references/>

Category:GO:0043488 ! regulation of mRNA stability

2012-02-16T12:44:35Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0043488_!_regulation_of_mRNA_stability}}

==References==
{{RefHelp}}
<references/>

PMID:17557827

2012-02-16T08:14:22Z

38.101.148.126: Fill PMID: Page!

{{RightTOC}}
<protect>
 '''Li, J, Attila, C, Wang, L, Wood, TK, Valdes, JJ and Bentley, WE''' (2007) Quorum sensing in Escherichia coli is signaled by AI-2/LsrR: effects on small RNA and biofilm architecture.''J. Bacteriol.'' '''189''':6011-20

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>The regulatory network for the uptake of Escherichia coli autoinducer 2 (AI-2) is comprised of a transporter complex, LsrABCD; its repressor, LsrR; and a cognate signal kinase, LsrK. This network is an integral part of the AI-2 quorum-sensing (QS) system. Because LsrR and LsrK directly regulate AI-2 uptake, we hypothesized that they might play a wider role in regulating other QS-related cellular functions. In this study, we characterized physiological changes due to the genomic deletion of lsrR and lsrK. We discovered that many genes were coregulated by lsrK and lsrR but in a distinctly different manner than that for the lsr operon (where LsrR serves as a repressor that is derepressed by the binding of phospho-AI-2 to the LsrR protein). An extended model for AI-2 signaling that is consistent with all current data on AI-2, LuxS, and the LuxS regulon is proposed. Additionally, we found that both the quantity and architecture of biofilms were regulated by this distinct mechanism, as lsrK and lsrR knockouts behaved identically. Similar biofilm architectures probably resulted from the concerted response of a set of genes including flu and wza, the expression of which is influenced by lsrRK. We also found for the first time that the generation of several small RNAs (including DsrA, which was previously linked to QS systems in Vibrio harveyi) was affected by LsrR. Our results suggest that AI-2 is indeed a QS signal in E. coli, especially when it acts through the transcriptional regulator LsrR.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' ||
* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17557827 PubMed]
Online version:[http://dx.doi.org/10.1128/JB.00014-07 10.1128/JB.00014-07]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{| id="K4f3cbadc84c0b" class=" tableEdit GO_table_reference dataTable"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.180905.K4f3cbadc84c0b&page=180905&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==See also==

==References==
{{RefHelp}}
<references/>

PMID:17557827

2012-02-16T08:14:14Z

38.101.148.126: New PMID: Page!

Category:GO:0005337 ! nucleoside transmembrane transporter activity

2012-02-16T07:21:52Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0005337_!_nucleoside_transmembrane_transporter_activity}}

==References==
{{RefHelp}}
<references/>

Category:GO:0004540 ! ribonuclease activity

2012-02-15T19:21:11Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004540_!_ribonuclease_activity}}

==References==
{{RefHelp}}
<references/>

Category:GO:0003987 ! acetate-CoA ligase activity

2012-02-15T04:35:43Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0003987_!_acetate-CoA_ligase_activity}}

==References==
{{RefHelp}}
<references/>

Category:GO:0042939 ! tripeptide transport

2012-02-15T03:57:41Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0042939_!_tripeptide_transport}}

==References==
{{RefHelp}}
<references/>

Category:GO:0004591 ! oxoglutarate dehydrogenase (succinyl-transferring) activity

2012-02-14T22:11:24Z

38.101.148.126: New GO term category page

{{GO term stub|GO:0004591_!_oxoglutarate_dehydrogenase_(succinyl-transferring)_activity}}

==References==
{{RefHelp}}
<references/>