Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery

被引:67
作者
Banci, Lucia [1 ,2 ]
Bertini, Ivano [1 ,2 ]
Ciofi-Baffoni, Simone [1 ,2 ]
Boscaro, Francesca [3 ]
Chatzi, Afroditi [4 ,5 ]
Mikolajczyk, Maciej [1 ,2 ]
Tokatlidis, Kostas [4 ,6 ]
Winkelmann, Julia [1 ,2 ]
机构
[1] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Florence, Italy
[2] Univ Florence, Dept Chem, I-50019 Florence, Italy
[3] Univ Florence, CISM, I-50139 Florence, Italy
[4] Fdn Res & Technol Hellas IMBB FORTH, Inst Mol Biol & Biotechnol, Iraklion 70013, Crete, Greece
[5] Univ Crete, Dept Biol, Iraklion 71409, Crete, Greece
[6] Univ Crete, Dept Mat Sci & Technol, Iraklion 71003, Crete, Greece
来源
CHEMISTRY & BIOLOGY | 2011年 / 18卷 / 06期
关键词
IRON-SULFUR CLUSTER; THERMOTOGA-MARITIMA ISCU; CYTOSOLIC FE/S PROTEINS; INTERMEMBRANE SPACE; DEPENDENT METHYLTRANSFERASES; MAGNETIC-RESONANCE; SCAFFOLD PROTEIN; NONHEME IRON; HUMAN NFU; BIOGENESIS;
D O I
10.1016/j.chembiol.2011.03.015
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
Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX(2)C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS.
引用
收藏
页码:794 / 804
页数:11
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