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Review
. 2005:59:211-31.
doi: 10.1146/annurev.micro.59.030804.121316.

Cellular functions, mechanism of action, and regulation of FtsH protease

Koreaki Ito  1 , Yoshinori Akiyama
Affiliations
Review

Cellular functions, mechanism of action, and regulation of FtsH protease

Koreaki Ito et al. Annu Rev Microbiol. 2005.

Abstract

FtsH is a cytoplasmic membrane protein that has N-terminally located transmembrane segments and a main cytosolic region consisting of AAA-ATPase and Zn2+-metalloprotease domains. It forms a homo-hexamer, which is further complexed with an oligomer of the membrane-bound modulating factor HflKC. FtsH degrades a set of short-lived proteins, enabling cellular regulation at the level of protein stability. FtsH also degrades some misassembled membrane proteins, contributing to their quality maintenance. It is an energy-utilizing and processive endopeptidase with a special ability to dislocate membrane protein substrates out of the membrane, for which its own membrane-embedded nature is essential. We discuss structure-function relationships of this intriguing enzyme, including the way it recognizes the soluble and membrane-integrated substrates differentially, on the basis of the solved structure of the ATPase domain as well as extensive biochemical and genetic information accumulated in the past decade on this enzyme.

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