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3' poly(A) is dispensable for translation.


In wild-type cells, the 3' poly(A) structure is necessary for translation of mRNA and for mRNA stability. The superkiller 2 (ski2), ski3, ski6, ski7, and ski8 mutations enhance the expression of the poly(A)(-) mRNAs of yeast RNA viruses. Ski2p is a DEVH-box RNA helicase and Slh1p resembles Ski2p. Both repress L-A double-stranded RNA (dsRNA) virus copy number, further suggesting that their functions may overlap. We find that slh1Delta ski2Delta double mutants are healthy (in the absence of viruses) and show normal rates of turnover of several cellular mRNAs. The slh1Delta ski2Delta strains translate electroporated nonpoly(A) mRNA with the same kinetics as polyA(+) mRNA. Thus, the translation apparatus is inherently capable of efficiently using nonpoly(A) mRNA even in the presence of normal amounts of competing poly(A)(+) mRNA, but is normally prevented from doing so by the combined action of the nonessential proteins Ski2p and Slh1p.

Pubmed ID: 10922069


  • Searfoss AM
  • Wickner RB


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

August 1, 2000

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Exoribonucleases
  • Exosome Multienzyme Ribonuclease Complex
  • Fungal Proteins
  • Phosphoglycerate Kinase
  • Poly A
  • Protein Biosynthesis
  • RNA, Messenger
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins