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PMID:19959836

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Contents

Citation

Price, CE and Driessen, AJ (2010) Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion. J. Biol. Chem. 285:3575-81

Abstract

All members of the Oxa1/Alb3/YidC family have been implicated in the biogenesis of respiratory and energy transducing proteins. In Escherichia coli, YidC functions together with and independently of the Sec system. Although the range of proteins shown to be dependent on YidC continues to increase, the exact role of YidC in insertion remains enigmatic. Here we show that YidC is essential for the insertion of subunit K of the NADH:ubiquinone oxidoreductase and that the dependence is due to the presence of two conserved glutamate residues in the transmembrane segments of subunit K. The results suggest a model in which YidC serves as a membrane chaperone for the insertion of the less hydrophobic, negatively charged transmembrane segments of NuoK.

Links

PubMed PMC2823498 Online version:10.1074/jbc.M109.051128

Keywords

Amino Acid Substitution; Blotting, Western; Cell Membrane/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Glutamates/genetics; Glutamates/metabolism; Lysine/genetics; Lysine/metabolism; Membrane Transport Proteins/genetics; Membrane Transport Proteins/metabolism; Mutation; NADH Dehydrogenase/genetics; NADH Dehydrogenase/metabolism; Protein Binding; Proteolipids/metabolism

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Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status

nuoK:Gene_Product(s)

GO:0005515

protein binding

IPI: Inferred from Physical Interaction

UniProtKB:P25714

F

Seeded from EcoCyc (v14.0)

complete

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References

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