The key to unlock the Hsp100/Clp protein degradation machines of Mycobacterium

authored by

Noël Molière, Kürşad Turgay

Abstract

Hsp100/Clp protease complexes are molecular machines important for cellular protein homeostasis and are concurrently embedded in the control of various signal transduction networks by regulatory proteolysis. In Mycobacteria, the genes encoding the components of these Hsp100/Clp protease complexes are essential for growth and were identified as targets for antibiotics, with a new antimicrobial mechanism, that are active on slow growing or even dormant cells. Schmitz and Sauer (2014) report the biochemical characterization of mycobacterial Hsp100/Clp protease complexes actively degrading folded substrate proteins. Their results suggest an unusual activation mechanism for this protease complex and will set the stage for further mechanistic studies of antibiotics acting on this new cellular target. Copyright

Organisation(s)

Institute of Microbiology

Type

Comment/debate

Journal

Molecular microbiology

Volume

93

Pages

583-586

No. of pages

4

ISSN

0950-382X

Publication date

30.06.2014

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Microbiology, Molecular Biology

Electronic version(s)

https://doi.org/10.1111/mmi.12696 (Access: Closed)