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ヨコヤマ ケン
YOKOYAMA KEN
横山 謙 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 | 2011/03 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Resolving stepping rotation in Thermus thermophilus H+-ATPase/synthase with an essentially drag-free probe |
| 執筆形態 | その他 |
| 掲載誌名 | NATURE COMMUNICATIONS |
| 出版社・発行元 | NATURE PUBLISHING GROUP |
| 巻・号・頁 | 2,pp.233 |
| 著者・共著者 | Shou Furuike,Masahiro Nakano,Kengo Adachi,Hiroyuki Noji,Kazuhiko Kinosita,Ken Yokoyama |
| 概要 | Vacuole-type ATPases (VoV1) and FoF1 ATP synthases couple ATP hydrolysis/synthesis in the soluble V-1 or F-1 portion with proton (or Na+) flow in the membrane-embedded V-o or F-o portion through rotation of one common shaft. Here we show at submillisecond resolutions the ATP-driven rotation of isolated V-1 and the whole VoV1 from Thermus thermophilus, by attaching a 40-nm gold bead for which viscous drag is almost negligible. V-1 made 120 steps, commensurate with the presence of three catalytic sites. Dwells between the steps involved at least two events other than ATP binding, one likely to be ATP hydrolysis. VoV1 exhibited 12 dwell positions per revolution, consistent with the 12-fold symmetry of the V-o rotor in T. thermophilus. Unlike F-1 that undergoes 80 degrees-40 degrees substepping, chemo-mechanical checkpoints in isolated V-1 are all at the ATP-waiting position, and V-o adds further bumps through stator-rotor interactions outside and remote from V-1. |
| DOI | 10.1038/ncomms1215 |
| ISSN | 2041-1723 |
| PMID | 21407199 |