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J Biol Chem. 2010 Feb 5;285(6):3575-81. doi: 10.1074/jbc.M109.051128. Epub 2009 Dec 3.

Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion.

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  • 1Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands.


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.

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