Both subunits of U2AF recognize the 3' splice site in Caenorhabditis elegans
Article Abstract:
It has been established that both of the subunits of the essential heterodimeric splicing factor U2AF are involved in RNA binding. U2AF65 crosslinks to RNA containing the U4C without the AG/R, while U2AF35 crosslinks to RNA only if the complete U4CAGR motif is present. U2AF from different organisms may recognize RNA differently, but U2AF could recognize the 3' splice site in other organisms in the same way as in Caenorhabditis elegans. It is suggested that those introns that do not need AG for the first stage of splicing have binding sites strong enough for U2AF65 for the additional binding energy supplied by the interaction of U2AF35 with AG/R not to be needed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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A protein related to splicing factor U2AF 35 that interacts with U2AF 65 and SR proteins in splicing of pre-mRNA
Article Abstract:
The function of a U2AF 35-related protein (Urp), the human homologue of a mouse imprinted gene, is described. Binding studies shows that Urp interacts specifically with U2AF 65 via a U2AF 350 homologous region and with SR proteins via the RS domain. This suggests that Urp and U2AF 35 could position RS-domain-containing factors independently with spliceosomes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Sex lethal controls dosage compensation in Drosophila by a non-spicing mechanism
Article Abstract:
Genetic research indicates female-specific ribonucleic acid-binding (RNA) sex lethal protein (SXL), which controls messenger RNA splicing in Drosophila, is also able to repress the translation of RNA transcripts in the process of sex determination. Deoxyribonucleic acid genetic sequences, photographs and diagrams illustrate the research findings.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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