Unrip is a component of SMN complexes active in snRNP assembly

被引:66
作者
Carissimi, C
Baccon, J
Straccia, M
Chiarella, P
Maiolica, A
Sawyer, A
Rappsilber, J
Pellizzoni, L [1 ]
机构
[1] CNR, Inst Cell Biol, Dulbecco Telethon Inst, I-00016 Rome, Italy
[2] Univ Penn, Sch Med, Philadelphia, PA 19104 USA
[3] EMBL, Monoclonal Antibody Core Facil, I-00016 Rome, Italy
[4] FIRC, Inst Mol Oncol Fdn, I-20139 Milan, Italy
来源
FEBS LETTERS | 2005年 / 579卷 / 11期
关键词
survival of motor neurons; spinal muscular atrophy; small nuclear ribonucleoprotein; unr-interacting protein;
D O I
10.1016/j.febslet.2005.03.034
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
A macromolecular complex containing survival of motor neurons (SMN), the spinal muscular atrophy protein, and Gemin2-7 interacts with Sm proteins and snRNAs to carry out the assembly of these components into spliceosomal small nuclear ribonucleoproteins (snRNPs). Here we report the characterization of unr-interacting protein (unrip), a GH-WD protein of unknown function, as a component of the SMN complex that interacts directly with Gemin6 and Gemin7. Unrip also binds a subset of Sm proteins, and unrip-containing SMN complexes are necessary and sufficient to mediate the assembly of spliceosomal snRNPs. These results demonstrate that unrip functions in the pathway of snRNP biogenesis and is a marker of cellular SMN complexes active in snRNP assembly. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2348 / 2354
页数:7
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