PUF60: a novel U2AF65-related splicing activity.

Page-McCaw PS, Amonlirdviman K, Sharp PA
RNA. 1999 5 (12): 1548-60

PMID: 10606266 · PMCID: PMC1369877 · DOI:10.1017/s1355838299991938

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.

MeSH Terms (19)

Amino Acid Sequence Cell Nucleus Chromatography, Affinity HeLa Cells Humans Molecular Sequence Data Monomeric GTP-Binding Proteins NM23 Nucleoside Diphosphate Kinases Nuclear Proteins Nucleoside-Diphosphate Kinase Poly U Ribonucleoproteins RNA-Binding Proteins RNA Splicing Sequence Alignment Sequence Homology, Amino Acid Serine-Arginine Splicing Factors Splicing Factor U2AF Transcription Factors

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