Specific commitment of different pre-mRNAs to splicing by single SR proteins
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.
- Publication:
-
Nature
- Pub Date:
- September 1993
- DOI:
- 10.1038/365082a0
- Bibcode:
- 1993Natur.365...82F