PMID:15910274
| Citation |
Ito, K and Akiyama, Y (2005) Cellular functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbiol. 59:211-31 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1146/annurev.micro.59.030804.121316 |
| Keywords |
ATP-Dependent Proteases; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Structure-Activity Relationship; Substrate Specificity |
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