Partial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA splicing factor required for pre-spliceosome assembly

被引：58

作者：

Caspary, F ^{[1
]}

Shevchenko, A ^{[1
]}

Wilm, M ^{[1
]}

Séraphin, B ^{[1
]}

机构：

[1] EMBL, D-69117 Heidelberg, Germany

来源：

EMBO JOURNAL | 1999年 / 18卷 / 12期

关键词：

DNA repair; polyadenylation; RSE1; Saccharomyces cerevisiae; SF3;

D O I：

10.1093/emboj/18.12.3463

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：

We have partially purified the U2 snRNP of Saccharomyces cerevisiae. Identification of some proteins consistently found in the purified fractions by nanoelectrospray mass spectrometry indicated the presence of a novel splicing factor named Rse1p. The RSE1 gene is essential and codes for a 148.2 kDa protein. We demonstrated that Rse1p associates specifically with U2 snRNA at low salt concentrations. In addition, we showed that Rse1p is a component of the prespliceosome. Depletion of Rse1p and analysis of a conditional mutant indicated that Rse1p was required for efficient splicing in vivo. In vitro Rse1p is required for the formation of pre-spliceosomes. Database searches revealed that Rse1p is conserved in humans and that it belongs to a large protein family that includes polyadenylation factors and DNA repair proteins. The characteristics of Rse1p suggest that its human homologue could be a subunit of the SF3 splicing factor.

引用

页码：3463 / 3474

页数：12

共 70 条

[1] THE YEAST MUD2 PROTEIN - AN INTERACTION WITH PRP11 DEFINES A BRIDGE BETWEEN COMMITMENT COMPLEXES AND U2 SNRNP ADDITION [J].