Yeast MAK3 N-acetyltransferase recognizes the N-terminal four amino acids of the major coat protein (gag) of the L-A double-stranded RNA virus

J Bacteriol. 1993 May;175(10):3192-4. doi: 10.1128/jb.175.10.3192-3194.1993.

Abstract

The MAK3 gene of Saccharomyces cerevisiae encodes an N-acetyltransferase whose acetylation of the N terminus of the L-A double-stranded RNA virus major coat protein (gag) is necessary for viral assembly. We show that the first 4 amino acids of the L-A gag protein sequence, MLRF, are a portable signal for N-terminal acetylation by MAK3. Amino acids 2, 3, and 4 are each important for acetylation by the MAK3 enzyme. In yeast cells, only three mitochondrial proteins are known to have the MAK3 acetylation signal, suggesting an explanation for the slow growth of mak3 mutants on nonfermentable carbon sources.

MeSH terms

  • Acetylation
  • Acetyltransferases / genetics*
  • Amino Acid Sequence
  • Arylamine N-Acetyltransferase*
  • Base Sequence
  • Fungal Proteins / genetics*
  • Gene Products, gag / metabolism*
  • Molecular Sequence Data
  • Protein Processing, Post-Translational
  • RNA Viruses / metabolism*
  • RNA, Double-Stranded
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • beta-Galactosidase / genetics
  • beta-Galactosidase / metabolism

Substances

  • Fungal Proteins
  • Gene Products, gag
  • RNA, Double-Stranded
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • MAK3 protein, S cerevisiae
  • Arylamine N-Acetyltransferase
  • beta-Galactosidase