LsrR-binding site recognition and regulatory characteristics in Escherichia coli AI-2 quorum sensing.

Abstract:

:In quorum sensing (QS) process, bacteria regulate gene expression by utilizing small signaling molecules called autoinducers in response to a variety of environmental cues. Autoinducer 2 (AI-2), a QS signaling molecule proposed to be involved in interspecies communication, is produced by many species of gram-negative and gram-positive bacteria. In Escherichia coli and Salmonella typhimurium, the extracellular AI-2 is imported into the cell by a transporter encoded by the lsr operon. Upstream of the lsr operon, there is a divergently transcribed gene encoding LsrR, which was reported previously to repress the transcription of the lsr operon and itself. Here, we have demonstrated for the first time that LsrR represses the transcription of the lsr operon and itself by directly binding to their promoters using gel shift and DNase I footprinting assays. The beta-galactosidase reporter assays further suggest that two motifs in both the lsrR and lsrA promoter regions are crucial for the LsrR binding. Furthermore, in agreement with the conclusion that phosphorylated AI-2 can relieve the repression of LsrR in previous studies, our data show that phospho-AI-2 renders LsrR unable to bind to its own promoter in vitro.

journal_name

Cell Res

journal_title

Cell research

authors

Xue T,Zhao L,Sun H,Zhou X,Sun B

doi

10.1038/cr.2009.91

subject

Has Abstract

pub_date

2009-11-01 00:00:00

pages

1258-68

issue

11

eissn

1001-0602

issn

1748-7838

pii

cr200991

journal_volume

19

pub_type

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