Format

Send to

Choose Destination
Mol Cell. 2003 Mar;11(3):659-69.

Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH.

Author information

1
Department of Microbiology & Immunology, University of California, San Franscisco, San Franscisco, CA 94143, USA. lherman@itsa.ucsf.edu

Abstract

FtsH, a member of the AAA family of proteins, is the only membrane ATP-dependent protease universally conserved in prokaryotes, and the only essential ATP-dependent protease in Escherichia coli. We investigated the mechanism of degradation by FtsH. Other well-studied ATP-dependent proteases use ATP to unfold their substrates. In contrast, both in vitro and in vivo studies indicate that degradation by FtsH occurs efficiently only when the substrate is a protein of low intrinsic thermodynamic stability. Because FtsH lacks robust unfoldase activity, it is able to use the protein folding state of substrates as a criterion for degradation. This feature may be key to its role in the cell and account for its ubiquitous distribution among prokaryotic organisms.

PMID:
12667449
DOI:
10.1016/s1097-2765(03)00068-6
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center