What nuclease cleaves pre-mRNA in the process of polyadenylation?

被引：9

作者：

Zarudnaya, MI ^{[1
]}

Kolomiets, IM ^{[1
]}

Hovorun, DM ^{[1
]}

机构：

[1] Natl Acad Sci Ukraine, Inst Mol Biol & Genet, UA-03143 Kiev, Ukraine

来源：

IUBMB LIFE | 2002年 / 54卷 / 01期

关键词：

CLP; CPSF-30; endonuclease; polyadenylation; Yth; 1p;

D O I：

10.1080/15216540213821

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：

A transcript-specific cleavage by a large set of proteins is the first stage of eukaryotic pre-mRNA polyadenylation. The main participant of this reaction-endonuclease-has not been discovered until now. However, mammalian CPSF-30 and yeast Yth 1p proteins are known to be homologues to Drosophila Clipper (CLP) protein, which possesses endoribonucleolytic activity. In the N-terminal region, all three proteins contain five copies of the CCCH zinc finger motif associated with nucleolytic activity in the case of CLP. The literature data on these proteins are reviewed here. These data were shown not to contradict the hypothesis that CPSF-30 and its homologues are the actual nucleases that cleave pre-mRNA in the process of polyadenylation.

引用

页码：27 / 31

页数：5

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