期刊
MOLECULAR CELL
卷 49, 期 4, 页码 692-703出版社
CELL PRESS
DOI: 10.1016/j.molcel.2012.12.009
关键词
-
资金
- DFG [FI 573/7-1, CH 1098/1-1]
- RVZ
Small nuclear ribonucleoproteins (snRNPs) represent key constituents of major and minor spliceosonnes. snRNPs contain a common core, composed of seven Sm proteins bound to snRNA, which forms in a step-wise and factor-mediated reaction. The assembly chaperone pICIn initially mediates the formation of an otherwise unstable pentanneric Sm protein unit. This so-called 6S complex docks subsequently onto the SMN complex, which removes pICIn and enables the transfer of pre-assembled Sm proteins onto snRNA. X-ray crystallography and electron microscopy was used to investigate the structural basis of snRNP assembly. The 6S complex structure identifies pICIn as an Sm protein mimic, which enables the topological organization of the Sm pentamer in a closed ring. A second structure of 6S bound to the SMN complex components SMN and Gemin2 uncovers a plausible mechanism of pICIn elimination and Sm protein activation for snRNA binding. Our studies reveal how assembly factors facilitate formation of RNA-protein complexes in vivo.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据