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PUF60: A novel U2AF65-related splicing activity

Published online by Cambridge University Press:  28 August 2001

PATRICK SCHONLEBER PAGE-McCAW ,
KEVIN AMONLIRDVIMAN  and
PHILLIP A. SHARP
PATRICK SCHONLEBER PAGE-McCAW
Affiliation:
Center for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA Present address: Department of Physiology, University of California, San Francisco, 513 Parnassus Avenue, Box 0444, San Francisco, California 94131-0444, USA.
KEVIN AMONLIRDVIMAN
Affiliation:
Center for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA Present address: Department of Molecular & Cell Biology, University of California, Berkeley, 401 Barker Hall #3204, Berkeley, California 94720-3204, USA.
PHILLIP A. SHARP
Affiliation:
Center for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
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Abstract

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. PUF 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.

Keywords

p54PUF60pump domainpyrimidine tractRRMsplicing factorU2AF
Type
Research Article
Information
RNA , Volume 5 , Issue 12 , December 1999 , pp. 1548 - 1560
Copyright
1999 RNA Society

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