共 23 条
The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway
被引:54
作者:

Terziyska, Nadia
论文数: 0 引用数: 0
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机构: Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany

Grumbt, Barbara
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机构: Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany

Bien, Melanie
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机构: Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany

Neupert, Walter
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机构: Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany

Herrmann, Johannes M.
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机构: Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany

Hell, Kai
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机构: Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany
机构:
[1] Univ Munich, Adolf Butenandt Inst Physiol Chem, D-81377 Munich, Germany
[2] Univ Kaiserslautern, D-67663 Kaiserslautern, Germany
关键词:
protein import;
Mia40-import pathway;
sulfhydryl oxidase Erv1;
mitochondria;
disulfide bond;
D O I:
10.1016/j.febslet.2007.02.014
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 thiol oxidase Erv1 and the redox-regulated receptor Mia40/Tim4O are components of a disulfide relay system which mediates import of proteins into the intermembrane space (IMS) of mitochondria. Here we report that ErvI requires Mia40 for its import into mitochondria. After passage across the translocase of the mitochondrial outer membrane Ervl interacts via disullide bonds with Mia40. Erv1 does not contain twin "CX3C" or twin "CX9C" motifs which are crucial for import of typical substrates of this pathway and it does not need two "CX2C" motifs for import into mitochondria. Thus, Erv1 represents an unusual type of substrate of the Mia40-dependent import pathway. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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页码:1098 / 1102
页数:5
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