Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle X-ray scattering

被引：4
|
作者：
Dedic, Emil [1 ,3 ]
Seweryn, Paulina [1 ,3 ]
Jonstrup, Anette Thyssen [1 ,3 ]
Flygaard, Rasmus Koch [1 ,3 ]
Fedosova, Natalya U. [4 ]
Hoffmann, Soren Vronning [5 ]
Boesen, Thomas [2 ,3 ]
Brodersen, Ditlev Egeskov [1 ,3 ]
机构：
[1] Aarhus Univ, Ctr MRNP Biogenesis & Metab, DK-8000 Aarhus C, Denmark
[2] Aarhus Univ, Ctr Membrane Pumps Cells & Dis PUMPKIN, DK-8000 Aarhus C, Denmark
[3] Aarhus Univ, Dept Mol Biol & Genet, DK-8000 Aarhus C, Denmark
[4] Aarhus Univ, Dept Biomed, DK-8000 Aarhus C, Denmark
[5] Aarhus Univ, Dept Phys & Astron, Inst Storage Ring Facil ISA, DK-8000 Aarhus C, Denmark
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2014年 / 450卷 / 01期
基金：
新加坡国家研究基金会;
关键词：
Exosome; 3 '-5 ' nuclease; RNA turnover; RNA processing; snoRNA; Ribosomal RNA; EUKARYOTIC EXOSOME; CRYSTAL-STRUCTURE; SUBUNIT RRP6P; RNA EXOSOME; DOMAIN; PROTEIN; RRP47P; DEGRADATION; MUTANTS; PACKAGE;
D O I：
10.1016/j.bbrc.2014.06.032
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 RNase D-type 3'-5' exonuclease Rrp6p from Saccharomyces cerevisiae is a nuclear-specific cofactor of the RNA exosome and associates in vivo with Rrp47p (Lrplp). Here, we show using biochemistry and small-angle X-ray scattering (SAXS) that Rrp6p and Rrp47p associate into a stable, heterodimeric complex with an elongated shape consistent with binding of Rrp47p to the nuclease domain and opposite of the HRDC domain of Rrp6p. Rrp47p reduces the exonucleolytic activity of Rrp6p on both single-stranded and structured RNA substrates without significantly altering the affinity towards RNA or the ability of Rrp6p to degrade RNA secondary structure. (C) 2014 Elsevier Inc. All rights reserved.
引用
收藏
页码：634 / 640
页数：7
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