A short helix in the C-terminal region of LolA is important for the specific membrane localization of lipoproteins

被引：24

作者：

Okuda, Suguru ^{[1
]}

Watanabe, Shoji ^{[1
]}

Tokuda, Hajime ^{[1
]}

机构：

[1] Univ Tokyo, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 1130032, Japan

来源：

FEBS LETTERS | 2008年 / 582卷 / 15期

关键词：

lipoprotein; molecular chaperone; outer membrane; periplasm; LolA; Escherichia coli;

D O I：

10.1016/j.febslet.2008.05.022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structures of a lipoprotein carrier, LolA, and a lipoprotein receptor, LolB, are similar except for an extra C-terminal loop containing a 3(10) helix and beta-strand 12 in LolA. Lipoprotein release was significantly reduced when beta-12 was deleted. Deletion of the 3(10) helix also inhibited the lipoprotein release. Furthermore, lipoproteins were non-specifically localized to membranes when LolA lacked the 3(10) helix. Thus, the membrane localization of lipoproteins with the LolA derivative lacking the 3(10) helix was independent of LolB whereas LolB was essential for the outer membrane localization of lipoproteins with the wild-type LolA. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2247 / 2251

页数：5

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