NDLI: LasR, a Transcriptional Activator of Pseudomonas aeruginosa Virulence Genes, Functions as a Multimer

Content Provider	PubMed Central
Author	Kiratisin, Pattarachai Tucker, Kenneth D. Luciano, Passador
Copyright Year	2002
Abstract	The Pseudomonas aeruginosa LasR protein functions in concert with N-3-oxo-dodecanoyl-l-homoserine lactone (3O-C12-HSL) to coordinate the expression of target genes, including many genes that encode virulence factors, with cell density. We used a LexA-based protein interaction assay to demonstrate that LasR forms multimers only when 3O-C12-HSL is present. A series of LasR molecules containing internal deletions or substitutions in single, conserved amino acid residues indicated that the N-terminal portion of LasR is required for multimerization. Studies performed with these mutant versions of LasR demonstrated that the ability of LasR to multimerize correlates with its ability to function as a transcriptional activator of lasI, a gene known to be tightly regulated by the LasR-3O-C12-HSL regulatory system. A LasR molecule that carries a C-terminal deletion can function as a dominant-negative mutant in P. aeruginosa, as shown by its ability to decrease expression of lasB, another LasR-3O-C12-HSL target gene. Taken together, our data strongly support the hypothesis that LasR functions as a multimer in vivo.
Related Links	http://dx.doi.org/10.1128/JB.184.17.4912-4919.2002
Starting Page	4912
File Format	PDF
ISSN	10985530
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	17
Volume Number	184
Language	English
Publisher	American Society for Microbiology
Publisher Date	2002-09-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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