PUF60: A novel U2AF65-related splicing activity

被引:109
作者
Page-McCaw, PS
Amonlirdviman, K
Sharp, PA
机构
[1] MIT, Ctr Canc Res, Cambridge, MA 02139 USA
[2] MIT, Dept Biol, Cambridge, MA 02139 USA
关键词
p54; PUF60; pump domain; pyrimidine tract; RRM; splicing factor; U2AF;
D O I
10.1017/S1355838299991938
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 identified a new pyrimidine-tract binding factor, PUF, that is required, together with U2AF, for efficient reconstitution of RNA splicing in vitro. The activity has been purified and consists of two proteins, PUF60 and the previously described splicing factor p54. p54 and PUF60 form a stable complex in vitro when cotranslated in a reaction mixture. PUP activity, in conjunction with U2AF, facilitates the association of U2 snRNP with the pre-mRNA, This reaction is dependent upon the presence of the large subunit of U2AF, U2AF65, but not the small subunit U2AF35, PUF60 is homologous to both U2AF65 and the yeast splicing factor Mud2p, The C-terminal domain of PUF60, the PUMP domain, is distantly related to the RNA-recognition motif domain, and is probably important in protein-protein interactions.
引用
收藏
页码:1548 / 1560
页数:13
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