The assembly of yeast mitochondrial ATP synthase: subunit depletion in vivo suggests ordered assembly of the stalk subunits b, OSCP and d

被引：24

作者：

Straffon, AFL ^{[1
]}

Prescott, M ^{[1
]}

Nagley, P ^{[1
]}

Devenish, RJ ^{[1
]}

机构：

[1] Monash Univ, Dept Biochem & Mol Biol, Melbourne, Vic 3168, Australia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 1998年 / 1371卷 / 02期

基金：

澳大利亚研究理事会;

关键词：

mitochondrion; ATP synthase; stalk region; assembly; subunit depletion; (yeast);

D O I：

10.1016/S0005-2736(98)00034-0

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：

The abundance in vivo of each of three subunits b, OSCP and ct, components of the stalk region of the yeast mitochondrial ATP synthase complex, was manipulated by a controlled depletion strategy. Western blots of whole cell lysates were used to study the effect of depletion of each of these subunits on the cellular levels of other subunits of the enzyme complex. A hierarchy of subunit stability was determined and interpreted to indicate the order of assembly of these three subunits of the stalk region. Thus, subunit b is assembled first, followed by OSCP and then by subunit d. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：157 / 162

页数：6

共 44 条

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[43] Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex
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[44] Assembly of the ribonucleoprotein complex containing the mRNA of the β-subunit of the mitochondrial H+-ATP synthase requires the participation of two distal cis-acting elements and a complex set of cellular trans-acting proteins
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