Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH.
Mol Cell
; 11(3): 659-69, 2003 Mar.
Article
en En
| MEDLINE
| ID: mdl-12667449
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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Factor sigma
/
Proteínas Bacterianas
/
Proteínas de la Membrana
Idioma:
En
Revista:
Mol Cell
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2003
Tipo del documento:
Article
País de afiliación:
Estados Unidos