Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters

被引：29

作者：

Abdrakhmanova, A ^{[1
]}

Dobrynin, K ^{[1
]}

Zwicker, K ^{[1
]}

Kerscher, S ^{[1
]}

Brandt, U ^{[1
]}

机构：

[1] Goethe Univ Frankfurt, Fachbereich Med, Zentrum Biol Chem, D-60590 Frankfurt, Germany

来源：

FEBS LETTERS | 2005年 / 579卷 / 30期

关键词：

thiosulfate : cyanide sulfurtransferase; electron transport complex I; protein association; mitochondria;

D O I：

10.1016/j.febslet.2005.11.008

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：

Here, we report that in the obligate aerobic yeast Yarrowia lipolytica, a protein exhibiting rhodanese (thiosulfate:cyanide sulfurtransferase) activity is associated with proton pumping NADH:ubiquinone oxidoreductase (complex I). Complex I is a key enzyme of the mitochondrial respiratory chain that contains eight iron-sulfur clusters. From a rhodanese deletion strain, we purified functional complex I that lacked the additional protein but was fully assembled and displayed no functional defects or changes in EPR signature. In contrast to previous suggestions, this indicated that the sulfurtransferase associated with Y. lipolytica complex I is not required for assembly of its iron-sulfur clusters. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：6781 / 6785

页数：5

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