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RseA, the SigE specific anti‐sigma factor of Mycobacterium tuberculosis , is inactivated by phosphorylation‐dependent ClpC1P2 proteolysis
Author(s) -
Barik Subhasis,
Sureka Kamakshi,
Mukherjee Partha,
Basu Joyoti,
Kundu Manikuntala
Publication year - 2010
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2009.07008.x
Subject(s) - regulon , sigma factor , biology , phosphorylation , microbiology and biotechnology , mycobacterium tuberculosis , proteolysis , cell envelope , regulator , gene , regulation of gene expression , biochemistry , promoter , gene expression , tuberculosis , enzyme , medicine , pathology , escherichia coli
Summary Central to the response of Mycobacterium tuberculosis to environmental stress is the regulation of genes under the control of alternative sigma factors. Sigma E of M. tuberculosis plays an important role in the intracellular life of the bacterium and regulates several genes which are important for maintaining the integrity of the cell envelope stress. This makes it important to understand how SigE is activated under stress. Here we elucidate the mechanisms regulating interaction of SigE with its cognate anti‐sigma factor RseA. Cysteines 70 and 73 are required for redox‐dependent interaction of RseA with SigE. Under surface stress, PknB‐dependent phosphorylation of RseA on T39 is required for its cleavage by ClpC1P2 thereby activating the SigE regulon. Rv2745c (MSMEG_2694), a transcriptional regulator, activates the clp regulon in response to vancomycin‐induced stress. Taken together with the previous report that Rv2745c is activated by SigE, our study uncovers a positive feedback loop that activates the sigE regulon under envelope stress.

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