跨膜亚基 K 中的 NADH：泛醌氧化还原酶的保守负电荷决定了其对 YidC 进行膜插入的依赖性。
Conserved negative charges in the transmembrane segments of subunit K of the NADH:ubiquinone oxidoreductase determine its dependence on YidC for membrane insertion.
机构信息
From the Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute for Advanced Materials, and the Kluyver Center for Genomics of Industrial Fermentation, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands.
From the Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute for Advanced Materials, and the Kluyver Center for Genomics of Industrial Fermentation, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands.
出版信息
J Biol Chem. 2010 Feb 5;285(6):3575-3581. doi: 10.1074/jbc.M109.051128. Epub 2009 Dec 3.
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.
Oxa1/Alb3/YidC 家族的所有成员都与呼吸和能量转导蛋白的生物发生有关。在大肠杆菌中，YidC 与 Sec 系统一起发挥作用，也可以独立发挥作用。尽管越来越多的蛋白质被证明依赖于 YidC，但 YidC 在插入过程中的确切作用仍然是个谜。在这里，我们表明 YidC 对于 NADH：泛醌氧化还原酶亚基 K 的插入是必不可少的，并且这种依赖性是由于亚基 K 的跨膜片段中存在两个保守的谷氨酸残基。结果表明，YidC 作为一种膜伴侣，用于插入 NuoK 的疏水性较小、带负电荷的跨膜片段。
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