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CELLULAR FUNCTIONS, MECHANISM OF ACTION, AND REGULATION OF FTSH PROTEASE
Abstract
FtsH is a cytoplasmic membrane protein that has N-terminally located transmembrane segments and a main cytosolic region consisting of AAA-ATPase and Zn 2+-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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EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS
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Metadata
- Authors
- Ito, K., & Akiyama, Y.
- Venue
- Annual Review of Microbiology
- Publisher
- Annual Reviews
- Published
- 2005-10-01
- Volume
- 59
- Issue
- 1
- Pages
- 211-231
- ISSN
- 0066-4227 (ISSN-L)
- 1545-3251
- OpenAlex
- W2160714701
- Cited by
- 436
- References
- 0
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ito, K., & Akiyama, Y. (2005). CELLULAR FUNCTIONS, MECHANISM OF ACTION, AND REGULATION OF FTSH PROTEASE. Annual Review of Microbiology. https://doi.org/10.1146/annurev.micro.59.030804.121316
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