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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 | 2014/01 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Molecular Basis of ADP Inhibition of Vacuolar (V)-type ATPase/Synthase |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF BIOLOGICAL CHEMISTRY |
| 出版社・発行元 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 巻・号・頁 | 289(1),pp.403-412 |
| 著者・共著者 | Jun-ichi Kishikawa,Atsuko Nakanishi,Shou Furuike,Masatada Tamakoshi,Ken Yokoyama |
| 概要 | Reduction of ATP hydrolysis activity of vacuolar-type ATPase/synthase (V0V1) as a result of ADP inhibition occurs as part of the normal mechanism of V0V1 of Thermus thermophilus but not V0V1 of Enterococcus hirae or eukaryotes. To investigate the molecular basis for this difference, domain-swapped chimeric V-1 consisting of both T. thermophilus and E. hirae enzymes were generated, and their function was analyzed. The data showed that the interaction between the nucleotide binding and C-terminal domains of the catalytic A subunit from E. hirae V-1 is central to increasing binding affinity of the chimeric V-1 for phosphate, resulting in reduction of the ADP inhibition. These findings together with a comparison of the crystal structures of T. thermophilus V-1 with E. hirae V-1 strongly suggest that the A subunit adopts a conformation in T. thermophilus V-1 different from that in E. hirae V-1. This key difference results in ADP inhibition of T. thermophilus V-1 by abolishing the binding affinity for phosphate during ATP hydrolysis. |
| DOI | 10.1074/jbc.M113.523498 |
| ISSN | 0021-9258/1083-351X |
| PMID | 24247239 |