Open AccessActivity Control of the ClpC Adaptor McsB in Bacillus subtilis
Author(s) -
Alexander K. W. Elsholz,
Kristina Hempel,
Stephan Michalik,
Katrin Gronau,
Dörte Becher,
Michael Hecker,
Ulf Gerth
Publication year - 2011
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00079-11
Subject(s) - bacillus subtilis , biology , signal transducing adaptor protein , bacterial protein , microbiology and biotechnology , computational biology , bacteria , genetics , signal transduction
Controlled protein degradation is an important cellular reaction for the fast and efficient adaptation of bacteria to ever-changing environmental conditions. In the low-GC, Gram-positive model organismBacillus subtilis , the AAA+ protein ClpC requires specific adaptor proteins not only for substrate recognition but also for chaperone activity. The McsB adaptor is activated particularly during heat stress, allowing the controlled degradation of the CtsR repressor by the ClpCP protease. Here we report how the McsB adaptor becomes activated by autophosphorylation on specific arginine residues during heat stress. In nonstressed cells McsB activity is inhibited by ClpC as well as YwlE.