| Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40. | |
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MedLine Citation:
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PMID: 17553782 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The mitochondrial intermembrane space (IMS) contains an essential machinery for protein import and assembly (MIA). Biogenesis of IMS proteins involves a disulfide relay between precursor proteins, the cysteine-rich IMS protein Mia40 and the sulfhydryl oxidase Erv1. How precursor proteins are specifically directed to the IMS has remained unknown. Here we systematically analyzed the role of cysteine residues in the biogenesis of the essential IMS chaperone complex Tim9-Tim10. Although each of the four cysteines of Tim9, as well as of Tim10, is required for assembly of the chaperone complex, only the most amino-terminal cysteine residue of each precursor is critical for translocation across the outer membrane and interaction with Mia40. Mia40 selectively recognizes cysteine-containing IMS proteins in a site-specific manner in organello and in vitro. Our results indicate that Mia40 acts as a trans receptor in the biogenesis of mitochondrial IMS proteins. |
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Authors:
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Dusanka Milenkovic; Kipros Gabriel; Bernard Guiard; Agnes Schulze-Specking; Nikolaus Pfanner; Agnieszka Chacinska |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2007-06-06 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 282 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2007 Aug |
Date Detail:
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Created Date: 2007-07-30 Completed Date: 2007-09-13 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 22472-80 Citation Subset: IM |
Affiliation:
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Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Universität Freiburg, D-79104 Freiburg, Germany. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Cysteine
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chemistry*,
metabolism Cystine / metabolism Disulfides Escherichia coli / metabolism Gene Expression Regulation, Fungal* Histidine / chemistry Membrane Proteins / metabolism* Membrane Transport Proteins / metabolism* Mitochondria / metabolism Mitochondrial Membrane Transport Proteins / metabolism* Mitochondrial Proteins / metabolism* Models, Genetic Oxidoreductases Acting on Sulfur Group Donors Protein Binding Protein Transport Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae Proteins / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Disulfides; 0/MRS11 protein, S cerevisiae; 0/Membrane Proteins; 0/Membrane Transport Proteins; 0/Mitochondrial Membrane Transport Proteins; 0/Mitochondrial Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Tim40 protein, S cerevisiae; 0/Tim9 protein, S cerevisiae; 52-90-4/Cysteine; 56-89-3/Cystine; 71-00-1/Histidine; EC 1.8.-/Oxidoreductases Acting on Sulfur Group Donors; EC 1.8.3.2/ERV1 protein, S cerevisiae |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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