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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-1-18
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pubmed:abstractText |
ProP is an integral membrane transporter of proline, glycine betaine, and several other osmoprotecting compounds. Fis plus RpoS collaborate to promote a burst of proP transcription in late exponential growth phase. This brief period of ProP synthesis enables stationary phase cells to cope with a potential hyperosmotic shock. Fis activates the RpoS (sigma(38))-dependent proP P2 promoter by binding to a site within the promoter region centered at -41 and thus functions as a class II activator. We show here that activation by Fis at this promoter is completely dependent upon the alpha-CTD of RNA polymerase and that the activation domain on Fis is localized to a four amino acid ridge on the surface of Fis adjacent to the helix-turn-helix DNA binding domain in only one subunit of the homodimer. Fis mutants containing amino acid substitutions within this region are defective in cooperative binding interactions with the sigma(38)-form of RNA polymerase. Some of these substitutions also alter interactions with DNA sequences flanking the core binding site, but we show that changes in Fis-mediated curvature do not affect promoter activity. We conclude that the same amino acids are used by Fis to activate transcription from a class I (-71, rrnB P1) and class II (-41, proP P2) location, but this region is distinct from that required to regulate the Hin site-specific DNA inversion reaction.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed RNA Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Factor For Inversion Stimulation...,
http://linkedlifedata.com/resource/pubmed/chemical/Integration Host Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ProP protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/RNA polymerase Esigma(38),
http://linkedlifedata.com/resource/pubmed/chemical/Sigma Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/sigma factor KatF protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
294
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
333-46
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10610762-Arginine,
pubmed-meshheading:10610762-Bacterial Proteins,
pubmed-meshheading:10610762-Binding Sites,
pubmed-meshheading:10610762-Carrier Proteins,
pubmed-meshheading:10610762-DNA-Binding Proteins,
pubmed-meshheading:10610762-DNA-Directed RNA Polymerases,
pubmed-meshheading:10610762-Dimerization,
pubmed-meshheading:10610762-Escherichia coli Proteins,
pubmed-meshheading:10610762-Factor For Inversion Stimulation Protein,
pubmed-meshheading:10610762-Integration Host Factors,
pubmed-meshheading:10610762-Models, Molecular,
pubmed-meshheading:10610762-Mutation,
pubmed-meshheading:10610762-Promoter Regions, Genetic,
pubmed-meshheading:10610762-Protein Conformation,
pubmed-meshheading:10610762-Sigma Factor,
pubmed-meshheading:10610762-Symporters,
pubmed-meshheading:10610762-Trans-Activators
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pubmed:year |
1999
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pubmed:articleTitle |
Localization of amino acids required for Fis to function as a class II transcriptional activator at the RpoS-dependent proP P2 promoter.
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pubmed:affiliation |
Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, CA 90095-1737, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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