The Effect of Ribosome Assembly Cofactors on In Vitro 30S Subunit Reconstitution

被引：61

作者：

Bunner, Anne E. ^{[1
,2
]}

Nord, Stefan ^{[3
]}

Wikstrom, Mikael ^{[3
]}

Williamson, James R. ^{[1
,2
]}

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

[3] Umea Univ, Dept Mol Biol, SE-90187 Umea, Sweden

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2010年 / 398卷 / 01期

基金：

美国国家卫生研究院;

关键词：

ribosome assembly; kinetics; Era; RimM; RimP/YhbC; DNAK CHAPERONE SYSTEM; ESCHERICHIA-COLI; CELL-CYCLE; BACTERIAL RIBOSOME; MATURATION PROTEIN; RNA; ERA; BIOGENESIS; BINDING; GTPASE;

D O I：

10.1016/j.jmb.2010.02.036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Ribosome biogenesis is facilitated by a growing list of assembly cofactors, including helicases, GTPases, chaperones, and other proteins, but the specific functions of many of these assembly cofactors are still unclear. The effect of three assembly cofactors on 30S ribosome assembly was determined in vitro using a previously developed mass-spectrometry-based method that monitors the rRNA binding kinetics of ribosomal proteins. The essential GTPase Era caused several late-binding proteins to bind rRNA faster when included in a 30S reconstitution. RimP enabled faster binding of S9 and S19 and inhibited the binding of S12 and S13, perhaps by blocking those proteins' binding sites. RimM caused proteins S5 and S12 to bind dramatically faster. These quantitative kinetic data provide important clues about the roles of these assembly cofactors in the mechanism of 30S biogenesis. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：1 / 7

页数：7

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