Abstract
Complex I (NADH:ubiquinone oxidoreductase) is the first and largest protein complex of the oxidative phosphorylation. Crystal structures have elucidated the positions of most subunits of bacterial evolutionary origin in the complex, but the positions of the eukaryotic subunits are unknown. Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx(9)C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8. We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8. We propose these subunits stabilize the membrane domain of complex I.
Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Biological Assay
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Cell Fractionation
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Cell Line
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Cloning, Molecular
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Disulfides / metabolism
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Electron Transport Complex I / metabolism*
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Electron Transport Complex I / ultrastructure
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Electrophoresis, Polyacrylamide Gel
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Endopeptidase K / metabolism
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Humans
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Iron-Sulfur Proteins / metabolism
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Mitochondrial Membranes / metabolism*
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Models, Molecular
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Molecular Sequence Data
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NADH Dehydrogenase / chemistry
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NADH Dehydrogenase / metabolism*
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NADH, NADPH Oxidoreductases / chemistry
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NADH, NADPH Oxidoreductases / metabolism*
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Oxidation-Reduction
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits / chemistry
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Protein Subunits / metabolism
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Sequence Alignment
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Surface Properties
Substances
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Disulfides
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Iron-Sulfur Proteins
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NDUFB7 protein, human
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Protein Subunits
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NADH, NADPH Oxidoreductases
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NADH Dehydrogenase
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Endopeptidase K
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Electron Transport Complex I
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NDUFA8 protein, human