γε sub-complex of thermophilic ATP synthase has the ability to bind ATP

被引：12

作者：

Iizuka, Satoshi

Kato, Shigeyuki

Yoshida, Masasuke

Kato-Yamada, Yasuyuki

机构：

[1] Rikkyo Univ, Coll Sci, Dept Life Sci, Toshima Ku, Tokyo 1718501, Japan

[2] Rikkyo Univ, Coll Sci, Frontier Project Adaptat & Evolut Extremophile, Tokyo 1718501, Japan

[3] Tokyo Inst Technol, Chem Resources Lab, Yokohama, Kanagawa 2268503, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 349卷 / 04期

关键词：

ATP binding; epsilon subunit; F-1; ATP synthase; FoF1;

D O I：

10.1016/j.bbrc.2006.09.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The isolated E; subunit of F-1-ATPase from thermophilic Bacillus PS3 (TF1) binds ATP [Y. Kato-Yamada, M. Yoshida, J. Biol. Chem. 278 (2003) 36013]. The obvious question is whether the ATP binding concern with the regulation of ATP synthase activity or not. If so, the F subunit even in the ATP synthase complex should have the ability to bind ATP. To check if the ATP binding to the F subunit within the ATP synthase complex may occur, the gamma epsilon sub-complex of TF1 was prepared and ATP binding was examined. The results clearly showed that the gamma epsilon sub-complex can bind ATP. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：1368 / 1371

页数：4

共 28 条

[1]

STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].