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Res Microbiol. 2009 Nov;160(9):618-28. doi: 10.1016/j.resmic.2009.08.006. Epub 2009 Sep 2.

Clp chaperone-proteases: structure and function.

Author information

1
ETH Zurich, Institute of Molecular Biology & Biophysics, Schafmattstrasse 20, 8093 Zurich, Switzerland.

Abstract

Clp proteases are the most widespread energy-dependent proteases in bacteria. Their two-component architecture of protease core and ATPase rings results in an inventory of several Clp protease complexes that often coexist. Here, we present insights into Clp protease function, from their assembly to substrate recruitment and processing, and how this is coupled to the expense of energy.

PMID:
19732826
DOI:
10.1016/j.resmic.2009.08.006
[Indexed for MEDLINE]

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