Related Experiment Video
Updated: Jun 1, 2026

Standardized Modular Assembly of Polycistronic Operons with Modular Cloning (MoClo) using the In-Cloning toolkit
Published on: September 2, 2025
Activity control of the ClpC adaptor McsB in Bacillus subtilis
A K W Elsholz1, K Hempel, S Michalik
1Institute of Microbiology, Ernst Moritz Arndt University Greifswald, Greifswald, Germany.
Abstract:
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 organism Bacillus 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.
Related Concept Videos
Coordination of Gene Expression Processes in Bacteria
Regulation of Bacterial Virulence
GPCRs Regulate Adenylyl Cylase Activity
Two...

