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PMID: 10220379 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Autoinducer binding by the quorum-sensing regulator TraR increases affinity for target promoters in vitro and decreases TraR turnover rates in whole cells.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 96 ·No. 9 ·1999-04-27 ·Pages 4832-7

Zhu J, Winans SC

Abstract

TraR is an Agrobacterium transcriptional regulator whose activity requires the pheromone N-3-oxooctanoyl-L-homoserine lactone. TraR was purified as a complex with the pheromone and contained one pheromone molecule per protein monomer. TraR-pheromone complexes bound to a single DNA site and activated two promoters that flank this site. Promoter expression was elevated 30-fold by using a supercoiled template. Pheromone binding increased the affinity of TraR for this binding site. Pheromone also increased TraR abundance in vivo by causing a 20-fold decrease in TraR turnover rates.

MeSH Terms
Bacterial Proteins/genetics DNA, Bacterial/genetics Gene Expression Regulation, Bacterial Homoserine/analogs & derivatives,genetics,metabolism Lactones/metabolism Pheromones/metabolism Promoter Regions, Genetic Rhizobium/genetics,metabolism Transcription Factors/genetics
Chemicals
Bacterial Proteins DNA, Bacterial Lactones Pheromones TraR protein, Agrobacterium tumefaciens Transcription Factors N-(beta-oxooctan-1-oyl)homoserine lactone Homoserine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zhu J
Section of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Winans S C
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26 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.96.9.4832
Published
1999-04-27
Pages
4832-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC21777
Subset
IM
Grants
NIGMS NIH HHS · R01 GM042893 · United States
NIGMS NIH HHS · GM42893 · United States
External Links
PubMed source DOI: 10.1073/pnas.96.9.4832 PMC Full Text View journal details
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