PUF60: A novel U2AF65-related splicing activity
Copyright policy )PUF60: A novel U2AF65-related splicing activity
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.
- University of California, Berkeley United States
- Massachusetts Institute of Technology United States
- University of California, San Francisco United States
Cell Nucleus, Poly U, Sequence Homology, Amino Acid, Serine-Arginine Splicing Factors, RNA Splicing, Molecular Sequence Data, Nuclear Proteins, RNA-Binding Proteins, NM23 Nucleoside Diphosphate Kinases, Splicing Factor U2AF, Chromatography, Affinity, Ribonucleoproteins, Nucleoside-Diphosphate Kinase, Humans, Amino Acid Sequence, Sequence Alignment, HeLa Cells, Monomeric GTP-Binding Proteins, Transcription Factors
Cell Nucleus, Poly U, Sequence Homology, Amino Acid, Serine-Arginine Splicing Factors, RNA Splicing, Molecular Sequence Data, Nuclear Proteins, RNA-Binding Proteins, NM23 Nucleoside Diphosphate Kinases, Splicing Factor U2AF, Chromatography, Affinity, Ribonucleoproteins, Nucleoside-Diphosphate Kinase, Humans, Amino Acid Sequence, Sequence Alignment, HeLa Cells, Monomeric GTP-Binding Proteins, Transcription Factors
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