Deciphering the assembly pathway of Sm-class U snRNPs

被引：88

作者：

Neuenkirchen, Nils ^{[1
]}

Chari, Ashwin ^{[1
]}

Fischer, Utz ^{[1
]}

机构：

[1] Univ Wurzburg, Chair Biochem, Theodor Boveri Inst, Bioctr, D-97074 Wurzburg, Germany

来源：

FEBS LETTERS | 2008年 / 582卷 / 14期

关键词：

U snRNP biogenesis; SMN-complex; PRMT5-complex; Sm proteins; splicing; U snRNA;

D O I：

10.1016/j.febslet.2008.03.009

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 assembly of the Sm-class of uridine-rich small nuclear ribonucleoproteins (U snRNPs), albeit spontaneous in vitro, has recently been shown to be dependent on the aid of a large number of assisting factors in vivo. These factors are organized in two interacting units termed survival motor neuron (SMN)- and protein arginine methyltransferase 5 (PRMT5)-complexes, respectively. While the PRMT5-complex acts early in the assembly pathway by activating common proteins of U snRNPs, the SMN-complex functions to join proteins and RNA in a highly ordered, apparently regulated manner. Here, we summarize recent progress in the understanding of this process and discuss the influence exerted by the aforementioned trans-acting factors. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1997 / 2003

页数：7

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