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 | 2005/12 |
形態種別 | 研究論文 |
査読 | 査読あり |
標題 | Rotation, structure, and classification of prokaryotic V-ATPase |
執筆形態 | その他 |
掲載誌名 | JOURNAL OF BIOENERGETICS AND BIOMEMBRANES |
出版社・発行元 | SPRINGER/PLENUM PUBLISHERS |
巻・号・頁 | 37(6),pp.405-410 |
著者・共著者 | K Yokoyama,H Imamura |
概要 | The prokaryotic V-type ATPase/synthases (prokaryotic V-ATPases) have simpler subunit compositions than eukaryotic V-ATPases, and thus are useful subjects for studying chemical, physical and structural properties of V-ATPase. In this review, we focus on the results of recent studies on the structure/function relationships in the V-ATPase from the eubacterium Thermus thermophilus. First, we describe single-molecule analyses of T.thermophilus V-ATPase. Using the single-molecule technique, it was established that the V-ATPase is a rotary motor. Second, we discuss arrangement of subunits in V-ATPase. Third, the crystal structure of the C-subunit (homolog of eukaryotic d-subunit) is described. This funnel-shape Subunit appears to cap the proteolipid ring in the V-0 domain in order to accommodate the V-1 central stalk. This structure seems essential for the regulatory reversible association/dissociation of the V-1 and the V-0 domains. Last, we discuss classification of the V-ATPase family. We propose that the term prokaryotic V-ATPases should be used rather than the term archaeal-type ATPase (A-ATPase). |
DOI | 10.1007/s10863-005-9480-1 |
ISSN | 0145-479X |
PMID | 16691473 |