Yeast mitochondrial F1F0-ATPase: the novel subunit e is identical Tim11

被引:63
作者
Arnold, I [1 ]
Bauer, MF [1 ]
Brunner, M [1 ]
Neupert, W [1 ]
Stuart, RA [1 ]
机构
[1] UNIV MUNICH,INST PHYSIOL CHEM,D-80336 MUNICH,GERMANY
关键词
mitochondrion; F1F0-ATPase; Tim11; intramitochondrial sorting;
D O I
10.1016/S0014-5793(97)00691-1
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
We report here the identification of the novel subunit of the mitochondrial F1F0-ATPase from Saccharomyces cerevisiae, ATPase subunit e. Yeast ATPase subunit e displays significant similarities in both amino acid sequence, properties (hydropathy and predicted coiled-coil structure) and orientation in the inner membrane,,vith previously identified mammalian ATPase subunit e proteins, Estimation of its native molecular mass and ability to be co-immunoprecipitated with a subunit of the F-1-ATPase, demonstrate that subunit e is a subunit of the F1F0-ATPase. Stable expression of subunit e requires the presence of the mitochondrially encoded subunits of the F-0-ATPase, Subunit e had been previously identified as Tim11 and was proposed to be involved in the process of sorting of proteins to the mitochondrial inner membrane. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:195 / 200
页数:6
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