Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria

被引：40

作者：

Chen, Ruming ^{[1
]}

Runswick, Michael J. ^{[1
]}

Carroll, Joe ^{[1
]}

Fearnley, Ian M. ^{[1
]}

Walker, John E. ^{[1
]}

机构：

[1] MRC, Dunn Human Nutr Unit, Cambridge CB2 0XY, England

来源：

FEBS LETTERS | 2007年 / 581卷 / 17期

基金：

英国医学研究理事会;

关键词：

mitochondria; ATP synthase; 6.8 kDa proteolipid; DAPIT; subunit composition; MEMBRANE DOMAIN; COMPLEX I; STALK; F1-ATPASE; PURIFICATION; F1F0-ATPASE; RESOLUTION; PROTEINS; SEQUENCE;

D O I：

10.1016/j.febslet.2007.05.079

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

ATP synthase, or F-ATPase, purified from bovine heart mitochondria in the absence of phospholipids is an assembly of 16 different subunits. In the presence of exogenous phospholipids, two additional hydrophobic proteins, a 6.8 kDa proteolipid and diabetes associated protein in insulin sensitive tissue (DAPIT), were associated with the purified complex, with DAPIT at sub-stoichiometric levels. Both proteins are conserved in vertebrates and invertebrates, but not in fungi, and prokaryotic F-ATPases do not contain orthologues of either of them. Therefore, their roles are likely to be peripheral to the synthesis of ATP. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3145 / 3148

页数：4

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