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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2003-12-3
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pubmed:abstractText |
The RhlR transcriptional regulator of Pseudomonas aeruginosa, along with its cognate autoinducer, N-butyryl homoserine lactone (C(4)-HSL), regulates gene expression in response to cell density. With an Escherichia coli LexA-based protein interaction system, we demonstrated that RhlR multimerized and that the degree of multimerization was dependent on the C(4)-HSL concentration. Studies with an E. coli lasB::lacZ lysogen demonstrated that RhlR multimerization was necessary for it to function as a transcriptional activator. Deletion analysis of RhlR indicated that the N-terminal domain of the protein is necessary for C(4)-HSL binding. Single amino acid substitutions in the C-terminal domain of RhlR generated mutant RhlR proteins that had the ability to bind C(4)-HSL and multimerize but were unable to activate lasB expression, demonstrating that the C-terminal domain is important for target gene activation. Single amino acid substitutions in both the N-terminal and C-terminal domains of RhlR demonstrated that both domains possess residues involved in multimerization. RhlR with a C-terminal deletion and an RhlR site-specific mutant form that possessed multimerization but not transcriptional activation capabilities were able to inhibit the ability of wild-type RhlR to activate rhlA expression in P. aeruginosa. We conclude that C(4)-HSL binding is necessary for RhlR multimerization and that RhlR functions as a multimer in P. aeruginosa.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-10430886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-10610820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-10617089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-10675332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-10960115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-11171981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-11226312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-11496014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12087407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12169617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12198141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12644476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12644477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12657054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-12657055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-1763027,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-2513561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-2762291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-3155268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-6769912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-7644517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-7836299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-7836318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-8522523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-9097014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-9150205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-9294432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-9491079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14645272-9821575
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
185
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7129-39
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14645272-4-Butyrolactone,
pubmed-meshheading:14645272-Bacterial Proteins,
pubmed-meshheading:14645272-Gene Expression Regulation, Bacterial,
pubmed-meshheading:14645272-Mutagenesis, Site-Directed,
pubmed-meshheading:14645272-Protein Structure, Tertiary,
pubmed-meshheading:14645272-Pseudomonas aeruginosa,
pubmed-meshheading:14645272-Serine Endopeptidases,
pubmed-meshheading:14645272-Transcriptional Activation
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pubmed:year |
2003
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pubmed:articleTitle |
Functional domains of the RhlR transcriptional regulator of Pseudomonas aeruginosa.
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pubmed:affiliation |
University of Rochester, Rochester, New York 14642, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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