POLYPEPTIDE COMPONENTS OF DROSOPHILA SMALL NUCLEAR RIBONUCLEOPROTEIN-PARTICLES

被引：26

作者：

PATERSON, T ^{[1
]}

BEGGS, JD ^{[1
]}

FINNEGAN, DJ ^{[1
]}

LUHRMANN, R ^{[1
]}

机构：

[1] KLINICUM PHILIPPS UNIV MARBURG,INST MOLEK BIOL & TUMORFORSCH,W-3550 MARBURG,GERMANY

来源：

NUCLEIC ACIDS RESEARCH | 1991年 / 19卷 / 21期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1093/nar/19.21.5877

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：

In eukaryotes splicing of pre-mRNAs is mediated by the spliceosome, a dynamic complex of small nuclear ribonucleoprotein particles (snRNPs) that associate transiently during spliceosome assembly and the splicing reaction. We have purified snRNPs from nuclear extracts of Drosophila cells by affinity chromatography with an antibody specific for the trimethylguanosine (m3G) cap structure of snRNAs U1-U5. The polypeptide components of Drosophila snRNPs have been characterized and shown to consist of a number of proteins shared by all the snRNPs, and some proteins which appear to be specific to individual snRNP particles. On the basis of their apparent molecular weight and antigenicity many of these common and particle specific Drosophila snRNP proteins are remarkably conserved between Drosophila and human spliceosomes. By probing western blots of the Drosophila snRNP polypeptides with a number of antisera raised against human snRNP proteins, Drosophila polypeptides equivalent to many of the HeLa snRNP-common proteins have been identified, as well as candidates for a number of U1, U2 and U5-specific proteins.

引用

页码：5877 / 5882

页数：6

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