Abstract
HIGHER eukaryotic cells express a family of essential splicing factors with a characteristic RNA-binding domain and serine arginine-rich (SR) motif1. These SR proteins, which include SC352–6 and SF2/ASF7–12, are conserved from Drosophila to man, are required for early steps of spliceosome assembly, and can influence splice-site selections. To address their mechanisms of action, SR proteins were examined for their role in committing pre-messenger RNA to the splicing pathway. I report here that SC35 was sufficient on its own to form a committed complex with human β-globin pre-mRNA. Examination of other SR proteins and pre-mRNA substrates revealed that single SR proteins committed different pre-mRNAs to splicing with pronounced substrate specificity. These results suggest that splicing of different pre-mRNAs may require distinct sets of SR proteins, and that the commitment by SR proteins may be a critical step at which alternative and tissue-specific splicing is regulated.
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Fu, XD. Specific commitment of different pre-mRNAs to splicing by single SR proteins. Nature 365, 82–85 (1993). https://doi.org/10.1038/365082a0
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DOI: https://doi.org/10.1038/365082a0
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