Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors

Nature. 1994 Mar 10;368(6467):119-24. doi: 10.1038/368119a0.

Abstract

Exactly how specific splice sites are recognized during the processing of complex precursor messenger RNAs is not clear. Small nuclear ribonucleoprotein particles (snRNPs) are involved, but are not sufficient by themselves to define splice sites. Now a human protein essential for splicing in vitro, called alternative splicing factor/splicing factor 2, is shown to cooperate with the U1 snRNP particle in binding pre-mRNA. This cooperation is probably achieved by specific interactions between the arginine/serine-rich domain of the splicing factor and a similar region in a U1 snRNP-specific protein.

Publication types

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

MeSH terms

  • Adenoviridae / genetics
  • Arginine / metabolism
  • HeLa Cells
  • Humans
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • RNA Precursors / metabolism*
  • RNA Splicing*
  • RNA, Viral / metabolism
  • RNA-Binding Proteins / metabolism*
  • Recombinant Proteins / metabolism
  • Ribonucleoprotein, U1 Small Nuclear / metabolism
  • Serine / metabolism
  • Serine-Arginine Splicing Factors

Substances

  • Nuclear Proteins
  • RNA Precursors
  • RNA, Viral
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Ribonucleoprotein, U1 Small Nuclear
  • Serine-Arginine Splicing Factors
  • Serine
  • Arginine