The C-terminal α-helix of YsxC is essential for its binding to 50S ribosome and rRNAs

被引：8

作者：

Wicker-Planquart, Catherine ^{[1
,2
,3
,4
]}

Ceres, Nicoletta ^{[5
]}

Jault, Jean-Michel ^{[1
,2
,3
,4
]}

机构：

[1] CNRS, IBS, F-38000 Grenoble, France

[2] Univ Grenoble Alpes, IBS, F-38027 Grenoble, France

[3] CNRS, IBS, F-38027 Grenoble, France

[4] CEA, DSV, IBS, F-38027 Grenoble, France

[5] Univ Lyon 1, BMSSI, UMR 5086, CNRS, F-69622 Villeurbanne, France

来源：

FEBS LETTERS | 2015年 / 589卷 / 16期

关键词：

YsxC; GTPase; Ribosome binding; Bacillus subtilis; PROTEIN; ERA; GTPASE; DOMAIN; IDENTIFICATION; SUBUNIT; GROWTH;

D O I：

10.1016/j.febslet.2015.06.006

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：

YsxC is an essential P-loop GTPase that interacts with the 50S subunit of the ribosome. The putative implication in ribosome binding of two basic clusters of YsxC, a conserved positively charged patch including R31, R116, H117 and K146 lying adjacent to the nucleotide-binding site, and the C-terminal alpha helix, was investigated. C-terminal truncation variants of YsxC were unable to bind to both ribosome and rRNAs, whereas mutations in the other cluster did not affect YsxC binding. Our results indicate that the basic C-terminal region of YsxC is required for its binding to the 50S ribosomal subunit. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2080 / 2086

页数：7

共 35 条

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