The α-helix of the second chromodomain of the 43 kDa subunit of the chloroplast signal recognition particle facilitates binding to the 54 kDa subunit

被引：21

作者：

Hermkes, Rebecca

Funke, Silke

Richter, Christine

Kuhlmann, Juergen

Schuenemann, Danja ^{[1
]}

机构：

[1] Ruhr Univ Bochum, Lehrstuhl Allgemeine & Mol Bot, D-44780 Bochum, Germany

[2] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany

来源：

FEBS LETTERS | 2006年 / 580卷 / 13期

关键词：

signal recognition particle; chloroplast; cpSRP43; chromodomain; protein transport;

D O I：

10.1016/j.febslet.2006.04.055

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：

Chloroplasts of higher plants contain a unique signal recognition particle (cpSRP) that consists of two proteins, cpSRP54 and cpSRP43. CpSRP43 is composed of a four ankyrin repeat domain and three functionally distinct chromodomains (CDs). In this report we confirm previously published data that the second chromodomain (CD2) provides the primary binding site for cpSRP54. However, quantitative binding analysis demonstrates that cpSRP54 binds to CD2 significantly less efficiently than it binds to full-length cpSRP43. Further analysis of the binding interface of cpSRP by mutagenesis studies and a pepscan approach demonstrates that the C-terminal alpha-helix of CD2 facilitates binding to cpSRP54. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3107 / 3111

页数：5

共 22 条

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