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チバ シノブ
CHIBA SHINOBU
千葉 志信 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2002/09 |
| 形態種別 | その他 |
| 標題 | Membrane protein degradation,by FtsH can be initiated from either end |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF BACTERIOLOGY |
| 出版社・発行元 | AMER SOC MICROBIOLOGY |
| 巻・号・頁 | 184(17),pp.4775-4782 |
| 著者・共著者 | S Chiba,Y Akiyama,K Ito |
| 概要 | FtsH, a membrane-bound metalloprotease, with cytoplasmic metalloprotease and AAA ATPase domains, degrades both soluble and integral membrane proteins in Escherichia coli. In this paper we investigated how membrane-embedded substrates are recognized by this enzyme. We showed previously that FtsH can initiate processive proteollysis at an N-terminal cytosolic tail of a membrane protein, by recognizing its length (more than 20 amino acid residues) but not exact sequence. Subsequent proteolysis should involve dislocation of the substrates into the cytosol. We now show that this enzyme can also initiate proteolysis at a C-terminal cytosolic tail and that the initiation efficiency depends on the length of the tail. This mode of degradation also appeared to be processive, which can be aborted by a tightly folded periplasmic domain. These results indicate that FtsH can exhibit processivity against membrane-embedded substrates in either the N-to-C or C-to-N direction. Our results also suggest that some membrane proteins receive bidirectional degradation simultaneously. These results raise intriguing questions about the molecular directionality of the dislocation and proteolysis catalyzed by FtsH. |
| DOI | 10.1128/JB.184.17.4775-4782.2002 |
| ISSN | 0021-9193 |