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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chacinska, Agnieszka Schulze-specking, Agnes Baker, Michael J. Ryan, Michael T. Pfanner, Nikolaus Müller, Judith M. Milenkovic, Dusanka Guiard, Bernard Gabriel, Kipros Stojanovski, Diana |
| Description | Author Affiliation: Stojanovski D ( Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Universität Freiburg, 79104 Freiburg, Germany.) |
| Abstract | The biogenesis of mitochondrial intermembrane space proteins depends on specific machinery that transfers disulfide bonds to precursor proteins. The machinery shares features with protein relays for disulfide bond formation in the bacterial periplasm and endoplasmic reticulum. A disulfide-generating enzyme/sulfhydryl oxidase oxidizes a disulfide carrier protein, which in turn transfers a disulfide to the substrate protein. Current views suggest that the disulfide carrier alternates between binding to the oxidase and the substrate. We have analyzed the cooperation of the disulfide relay components during import of precursors into mitochondria and identified a ternary complex of all three components. The ternary complex represents a transient and intermediate step in the oxidation of intermembrane space precursors, where the oxidase Erv1 promotes disulfide transfer to the precursor while both oxidase and precursor are associated with the disulfide carrier Mia40. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 2 |
| Volume Number | 183 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2008-10-20 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Disulfides Metabolism Mitochondria Enzymology Mitochondrial Membrane Transport Proteins Mitochondrial Proteins Multiprotein Complexes Oxidoreductases Protein Precursors Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Mutation Oxidation-Reduction Oxidoreductases Acting On Sulfur Group Donors Protein Binding Protein Transport Substrate Specificity Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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