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参与脂多糖外膜分选的ABC转运蛋白LptBFGC复合物的生化特性

Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides.

作者信息

Narita Shin-ichiro, Tokuda Hajime

机构信息

Institute of Molecular and Cellular Biosciences, University of Tokyo, Tokyo, Japan.

出版信息

FEBS Lett. 2009 Jul 7;583(13):2160-4. doi: 10.1016/j.febslet.2009.05.051. Epub 2009 Jun 3.

Abstract

Seven Lpt proteins (A through G) are thought to be involved in lipopolysaccharide transport from the inner to outer membrane of Escherichia coli. LptB belongs to the ATP-binding cassette transporter superfamily. Although the lptB gene lacks neighboring genes encoding membrane subunits, bioinformatic analyses recently indicated that two distantly located consecutive genes, lptF and lptG, could encode membrane subunits. To examine this possibility, LptB was expressed with LptF and LptG. We report here that both LptF and LptG formed a complex with LptB. Furthermore, an inner membrane protein, LptC, which had been implicated in lipopolysaccharide transport, was also included in this complex.

摘要

七种脂多糖转运蛋白(A至G)被认为参与了大肠杆菌脂多糖从内膜到外膜的转运过程。LptB属于ATP结合盒转运蛋白超家族。尽管lptB基因缺乏编码膜亚基的相邻基因,但最近的生物信息学分析表明,两个距离较远的连续基因lptF和lptG可能编码膜亚基。为了验证这种可能性,我们将LptB与LptF和LptG一起表达。我们在此报告,LptF和LptG均与LptB形成了复合物。此外,一种曾被认为与脂多糖转运有关的内膜蛋白LptC也包含在该复合物中。

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