Specific commitment of different pre-mRNAs to splicing by single SR proteins

Nature. 1993 Sep 2;365(6441):82-5. doi: 10.1038/365082a0.


Higher eukaryotic cells express a family of essential splicing factors with a characteristic RNA-binding domain and serine/arginine-rich (SR) motif. These SR proteins, which include SC35 and SF2/ASF, 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 beta-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 types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Baculoviridae
  • Binding, Competitive
  • Cell Line
  • Cloning, Molecular
  • Gene Products, tat / genetics
  • Globins / biosynthesis
  • Globins / genetics*
  • Heterogeneous-Nuclear Ribonucleoproteins
  • Humans
  • Moths
  • Nuclear Proteins / metabolism*
  • RNA Precursors / metabolism*
  • RNA Splicing*
  • RNA-Binding Proteins / metabolism*
  • Ribonucleoproteins / metabolism
  • Serine-Arginine Splicing Factors
  • Spliceosomes / metabolism


  • Gene Products, tat
  • Heterogeneous-Nuclear Ribonucleoproteins
  • Nuclear Proteins
  • RNA Precursors
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • SRSF2 protein, human
  • Serine-Arginine Splicing Factors
  • Globins