The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA

Mol Cell Biol. 1992 Aug;12(8):3390-8. doi: 10.1128/mcb.12.8.3390-3398.1992.


The eukaryotic mRNA 5' cap structure m7GpppX (where X is any nucleotide) interacts with a number of cellular proteins. Several of these proteins were studied in mammalian, yeast, and drosophila cells and found to be involved in translation initiation. Here we describe a novel cap-binding protein, the coat protein of L-A, a double-stranded RNA virus that is persistently maintained in many Saccharomyces cerevisiae strains. The results also suggest that the coat protein of a related double-stranded RNA virus (L-BC) is likewise a cap-binding protein. Strikingly, in contrast to the cellular cap-binding proteins, the interaction between the L-A virus coat protein and the cap structure is through a covalent bond.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Capsid / genetics
  • Capsid / isolation & purification
  • Capsid / metabolism*
  • Cyanogen Bromide
  • Genotype
  • Kinetics
  • Molecular Sequence Data
  • Peptide Fragments / isolation & purification
  • RNA Caps / metabolism*
  • RNA Viruses / genetics
  • RNA Viruses / metabolism*
  • RNA, Double-Stranded / genetics
  • RNA, Messenger / metabolism*
  • Ribonucleases
  • Ribosomes / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Sequence Homology, Nucleic Acid
  • Thermodynamics
  • Transcription, Genetic
  • Trypsin


  • Peptide Fragments
  • RNA Caps
  • RNA, Double-Stranded
  • RNA, Messenger
  • Ribonucleases
  • Trypsin
  • Cyanogen Bromide