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Vol. 95, Issue 15, 8721-8726, July 21, 1998
* Department of Molecular Genetics and Microbiology and
Edited by Fred Sherman, University of Rochester School of Medicine,
Rochester, NY, and approved May 28, 1998 (received for review March
30, 1998)
The nonsense-mediated mRNA decay pathway functions to degrade
aberrant mRNAs that contain premature translation termination codons.
In Saccharomyces cerevisiae, the Upf1, Upf2, and Upf3 proteins have been identified as trans-acting factors
involved in this pathway. Recent results have demonstrated that the Upf proteins may also be involved in maintaining the fidelity of several aspects of the translation process. Certain mutations in the
UPF1 gene have been shown to affect the efficiency of
translation termination at nonsense codons and/or the process of
programmed
Copyright © 1998 by The National Academy of Sciences 0027-8424/98/958721-6$2.00/0
Genetics
The Upf3 protein is a component of the surveillance
complex that monitors both translation and mRNA turnover and affects
viral propagation
,
,
,
,
, and
,§,¶
Graduate Program in Molecular Biosciences at University of
Medicine and Dentistry of New Jersey/Rutgers Universities, Robert
Wood Johnson Medical School-University of Medicine and Dentistry of
New Jersey, and § The Cancer Institute of New Jersey, 675 Hoes
Lane, Piscataway NJ 08854
1 ribosomal frameshifting used by viruses to control their
gene expression. Alteration of programmed frameshift efficiencies can
affect virus assembly leading to reduced viral titers or elimination of
the virus. Here we present evidence that the Upf3 protein also
functions to regulate programmed
1 frameshift efficiency. A
upf3-
strain demonstrates increased sensitivity to
the antibiotic paromomycin and increased programmed
1 ribosomal
frameshift efficiency resulting in loss of the M1 virus.
Based on these observations, we hypothesize that the Upf proteins are
part of a surveillance complex that functions to monitor translational
fidelity and mRNA turnover.
M.J.R.-E. and J.M.Y. contributed equally to this work.
¶
To whom reprint requests should be addressed. e-mail:
Peltz{at}RWJA.UMDNJ.EDU.
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