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1 Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, USA
2 Program in Molecular Biosciences at University of Medicine and Dentistry of New Jersey (UMDNJ)/Rutgers Universities, Piscataway New Jersey 08854, USA
Reprint requests to: Jonathan D. Dinman, Department of Cell Biology and Molecular Genetics, Microbiology Building, Room 2135, University of Maryland, College Park, MD 20742, USA; e-mail: dinman{at}umd.edu; fax: 301-314-9489.
Increased efficiencies of programmed -1 ribosomal frameshifting in yeast cells expressing mutant forms of ribosomal protein L3 are unable to maintain the dsRNA "Killer" virus. Here we demonstrate that changes in frameshifting and virus maintenance in these mutants correlates with decreased peptidyltransferase activities. The mutants did not affect Ty1-directed programmed +1 ribosomal frameshifting or nonsense-mediated mRNA decay. Independent experiments demonstrate similar programmed -1 ribosomal frameshifting specific defects in cells lacking ribosomal protein L41, which has previously been shown to result in peptidyltransferase defects in yeast. These findings are consistent with the hypothesis that decreased peptidyltransferase activity should result in longer ribosome pause times after the accommodation step of the elongation cycle, allowing more time for ribosomal slippage at programmed -1 ribosomal frameshift signals.
Keywords: Frameshifting; ribosome; virus
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