Analyzing the interaction of RseA and RseB, the two negative regulators of the sigmaE envelope stress response, using a combined bioinformatic and experimental strategy.

ABSTRACT: The Escherichia coli envelope stress response is controlled by the alternative sigma factor, sigma(E), and is induced when unfolded outer membrane proteins accumulate in the periplasm. The response is initiated by sequential cleavage of the membrane-spanning antisigma factor, RseA. RseB is an important negative regulator of envelope stress response that exerts its negative effects onsigma(E) activity through its binding to RseA. In this study, we analyze the interaction between RseA and RseB. We found that tight binding of RseB to RseA required intact RseB. Using programs that performed global and local sequence alignment of RseB and RseA, we found regions of high similarity and performed alanine substitution mutagenesis to test the hypothesis that these regions were functionally important

SUBMITTER: Ahuja N 

PROVIDER: S-EPMC2643490 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature