A conserved a helix of Bcs1, a mitochondrial AAA chaperone, is required for the Respiratory Complex III maturation
A conserved a helix of Bcs1, a mitochondrial AAA chaperone, is required for the Respiratory Complex III maturation
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呼吸复合物 III 成熟需要 Bcs1 的保守螺旋（线粒体 AAA 伴侣）
DOI：
10.1016/j.bbrc.2013.12.084
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发表时间：
2014
影响因子：
3.1
通讯作者：
Teru Ogura and Masatoshi Esaki
中科院分区：
文献类型：
--
作者：
Rie Sawamura;Teru Ogura and Masatoshi Esaki
Bcs 1是线粒体内膜中的跨膜伴侣，并且是线粒体呼吸链复合物III组装所需的。它已被证明，高度保守的C-末端区域的Bcs 1，包括AAA ATP酶结构域的矩阵侧是必不可少的伴侣功能。在这里，我们描述的重要性，N-末端的短片段位于膜间隙中的Bcs 1功能。在酵母Bcs 1的N-末端44个氨基酸残基中，前37个残基是疏水性的，而残基38中的疏水性氨基酸对于Rieske铁硫蛋白从线粒体基质整合到过早的复合物III中是必需的。用亲水性氨基酸残基取代残基38影响Bcs 1的构象和与其他蛋白质的相互作用。Bcs 1在膜间隙中进化保守的短α螺旋是分子伴侣功能的重要组成部分。
Bcs1 is a transmembrane chaperone in the mitochondrial inner membrane, and is required for the mitochondrial Respiratory Chain Complex III assembly. It has been shown that the highly-conserved C-terminal region of Bcs1 including the AAA ATPase domain in the matrix side is essential for the chaperone function. Here we describe the importance of the N-terminal short segment located in the intermembrane space in the Bcs1 function. Among the N-terminal 44 amino acid residues of yeast Bcs1, the first 37 residues are dispensable whereas a hydrophobic amino acid in the residue 38 is essential for integration of Rieske Iron-sulfur Protein into the premature Complex III from the mitochondrial matrix. Substitution of the residue 38 by a hydrophilic amino acid residue affects conformation of Bcs1 and interactions with other proteins. The evolutionarily-conserved short α helix of Bcs1 in the intermembrane space is an essential element for the chaperone function.