Literature DB >> 10606266

PUF60: a novel U2AF65-related splicing activity.

P S Page-McCaw1, K Amonlirdviman, P A Sharp.   

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.

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Year:  1999        PMID: 10606266      PMCID: PMC1369877          DOI: 10.1017/s1355838299991938

Source DB:  PubMed          Journal:  RNA        ISSN: 1355-8382            Impact factor:   4.942


  45 in total

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  62 in total

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7.  Genomic functions of U2AF in constitutive and regulated splicing.

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8.  Sequence, Structure, and Context Preferences of Human RNA Binding Proteins.

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9.  Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein.

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10.  Dual function for U2AF(35) in AG-dependent pre-mRNA splicing.

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