Binding to G-quadruplex RNA activates the mitochondrial GTPase NOA1

被引:15
作者
Al-Furoukh, Natalie [1 ]
Goffart, Steffi [1 ,2 ]
Szibor, Marten [1 ]
Wanrooij, Sjoerd [3 ,4 ]
Braun, Thomas [1 ]
机构
[1] Max Planck Inst Heart & Lung Res, D-61231 Bad Nauheim, Germany
[2] Univ Eastern Finland, Dept Biol, Joensuu 80101, Finland
[3] Univ Gothenburg, Dept Med Biochem & Cell Biol, SE-40530 Gothenburg, Sweden
[4] Washington Univ, Dept Biochem & Biophys, Burgers Lab, St Louis, MO 63110 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2013年 / 1833卷 / 12期
基金
瑞典研究理事会;
关键词
NOA1; G-quadruplex; Binding motif; GTPase; Aptamer; SELEX; RIBOSOMAL-SUBUNIT; TRANSCRIPTION TERMINATION; BACILLUS-SUBTILIS; DNA STRUCTURES; LON PROTEASE; YQEH; BIOGENESIS; PROTEINS; POLYADENYLATION; REPLICATION;
D O I
10.1016/j.bbamcr.2013.07.022
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
NOA1 is an evolutionary conserved, nuclear encoded GTPase essential for mitochondrial function and cellular survival. The function of NOA1 for assembly of mitochondrial ribosomes and regulation of OXPHOS activity depends on its GTPase activity, but so far no ligands have been identified that regulate the GTPase activity of NOA1. To identify nucleic acids that bind to the RNA-binding domain of NOA1 we employed SELEX (Systemic Evolution of Ligands by Exponential Enrichment) using recombinant mouse wildtype NOA1 and the GTPase mutant NOA1-K353R We found that NOA1 binds specifically to oligonucleotides that fold into guanine tetrads (G-quadruplexes). Binding of G-quadruplex oligonucleotides stimulated the GTPase activity of NOA1 suggesting a regulatory link between G-quadruplex containing RNAs, NOA1 function and assembly of mitochondrial ribosomes. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:2933 / 2942
页数:10
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