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The key to unlock the Hsp 100/ Clp protein degradation machines of M ycobacterium
Author(s) -
Molière Noël,
Turgay Kürşad
Publication year - 2014
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/mmi.12696
Subject(s) - biology , proteolysis , protease , ubiquitin , microbiology and biotechnology , gene , biochemistry , enzyme
Summary Hsp 100/ 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 M ycobacteria , the genes encoding the components of these Hsp 100/ 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 Hsp 100/ 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.