| Автор | Ito, Koreaki |
| Автор | Akiyama, Yoshinori |
| Дата выпуска | 2005 |
| dc.description | 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<sup>2+</sup>-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. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | CELLULAR FUNCTIONS, MECHANISM OF ACTION, AND REGULATION OF FTSH PROTEASE |
| DOI | 10.1146/annurev.micro.59.030804.121316 |
| Print ISSN | 0066-4227 |
| Журнал | Annual Review of Microbiology |
| Том | 59 |
| Первая страница | 211 |
| Последняя страница | 231 |
| Аффилиация | Ito, Koreaki; Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan; email: kito@virus.kyoto-u.ac.jp , yakiyama@virus.kyoto-u.ac.jp |
