Gene-protein assignments within the yeast Yarrowia lipolytica dsRNA viral genome

Curr Genet. 1987;11(6-7):483-90. doi: 10.1007/BF00384610.

Abstract

Some strains of the yeast Yarrowia lipolytica possess virus-like particles (VLPs) which encapsidate a double-stranded RNA (dsRNA) genome designated Ly. We report here that these VLPs have two associated polypeptides of molecular weights 83 kd (VLy-P1) and 77 kd (VLy-P2). Denatured Ly-dsRNA was used to program a cell-free rabbit reticulocyte translation system, resulting in the appearance of four major products, viz. Ly-P1 (83 kd); Ly-P2 (77 kd); Ly-P3 (74 kd) and Ly-P4 (68 kd). The in vivo viral-associated protein VLy-P1 co-migrated on SDS-polyacrylamide gels with the in vitro product Ly-P1 and, similarly, VLy-P2 co-migrated with Ly-P2. Peptide mapping data confirm the identity of the in vivo products (VLy-P1 and VLy-P2) and their in vitro counterparts. The conclusion made is that VLy-P1 and VLy-P2 are almost identical primary translation products of the Ly genome, derived from a single or multiple species of Ly-dsRNA. RNA blot hybridizations using L1A M1 and separately, L2A M2 probes prepared from appropriate K1 and K2 Saccharomyces cerevisiae killer strains, failed to show any detectable homology to Ly-dsRNA, substantiating the uniqueness of the Ly genome with respect to the K1 and K2 S. cerevisiae dsRNA killer systems.

Publication types

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

MeSH terms

  • Animals
  • Genes, Fungal*
  • Genes, Viral*
  • Genotype
  • Nucleic Acid Hybridization
  • Peptide Mapping
  • Phenotype
  • Protein Biosynthesis
  • RNA, Double-Stranded / genetics*
  • Rabbits
  • Reticulocytes / metabolism
  • Viral Proteins / genetics*
  • Viruses / genetics

Substances

  • RNA, Double-Stranded
  • Viral Proteins