Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.

Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.
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SM级核糖核蛋白的生物发生需要两个不同的精氨酸甲基转移酶。

DOI:
10.1083/jcb.200702147
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发表时间:
2007-08-27
影响因子:
7.8
通讯作者:
Matera, A. Gregory
Matera, A. Gregory
中科院分区:
生物学1区
文献类型:
--
作者:
Gonsalvez, Graydon B.;Tian, Liping;Ospina, Jason K.;Boisvert, Francois-Michel;Lamond, Angus I.;Matera, A. Gregory

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小核核糖核蛋白(snRNP)是剪接体的核心组成部分。U1、U2、U4和U 5 snRNP各自包含一组共有的7种Sm蛋白。这些Sm蛋白的三个postperturbationally修改包含对称的二甲基精氨酸(SDMA)残基在其C-末端的尾巴。然而,这种修饰在snRNP生物合成途径中的确切功能尚不清楚。一些证据表明,甲基转移酶蛋白精氨酸甲基转移酶5(PRMT 5)是负责Sm蛋白的sDMA修饰。我们发现,在人类细胞中,PRMT 5和一个新发现的II型甲基转移酶,PRMT 7,每个Sm蛋白sDMA修饰所需的。此外,我们表明,这两种酶的功能非冗余Sm蛋白甲基化。最后,我们提供了在体内的证据表明,Sm蛋白sDMA的修改所需的snRNP在人类细胞中的生物合成。
Small nuclear ribonucleoproteins (snRNPs) are core components of the spliceosome. The U1, U2, U4, and U5 snRNPs each contain a common set of seven Sm proteins. Three of these Sm proteins are posttranslationally modified to contain symmetric dimethylarginine (sDMA) residues within their C-terminal tails. However, the precise function of this modification in the snRNP biogenesis pathway is unclear. Several lines of evidence suggest that the methyltransferase protein arginine methyltransferase 5 (PRMT5) is responsible for sDMA modification of Sm proteins. We found that in human cells, PRMT5 and a newly discovered type II methyltransferase, PRMT7, are each required for Sm protein sDMA modification. Furthermore, we show that the two enzymes function nonredundantly in Sm protein methylation. Lastly, we provide in vivo evidence demonstrating that Sm protein sDMA modification is required for snRNP biogenesis in human cells.
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