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Molecular and Cellular Biology, July 2006, p. 5237-5248, Vol. 26, No. 14
0270-7306/06/$08.00+0     doi:10.1128/MCB.02448-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Tpa1p Is Part of an mRNP Complex That Influences Translation Termination, mRNA Deadenylation, and mRNA Turnover in Saccharomyces cerevisiae

Kim M. Keeling,1 Joe Salas-Marco,1,{dagger} Lev Z. Osherovich,2,{ddagger} and David M. Bedwell1*

Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama,1 Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, California2

Received 22 December 2005/ Returned for modification 30 January 2006/ Accepted 3 May 2006

In this report, we show that the Saccharomyces cerevisiae protein Tpa1p (for termination and polyadenylation) influences translation termination efficiency, mRNA poly(A) tail length, and mRNA stability. Tpa1p is encoded by the previously uncharacterized open reading frame YER049W. Yeast strains carrying a deletion of the TPA1 gene (tpa1{Delta}) exhibited increased readthrough of stop codons, and coimmunoprecipitation assays revealed that Tpa1p interacts with the translation termination factors eRF1 and eRF3. In addition, the tpa1{Delta} mutation led to a 1.5- to 2-fold increase in the half-lives of mRNAs degraded by the general 5'->3' pathway or the 3'->5' nonstop decay pathway. In contrast, this mutation did not have any affect on the nonsense-mediated mRNA decay pathway. Examination of mRNA poly(A) tail length revealed that poly(A) tails are longer than normal in a tpa1{Delta} strain. Consistent with a potential role in regulating poly(A) tail length, Tpa1p was also found to coimmunoprecipitate with the yeast poly(A) binding protein Pab1p. These results suggest that Tpa1p is a component of a messenger ribonucleoprotein complex bound to the 3' untranslated region of mRNAs that affects translation termination, deadenylation, and mRNA decay.

* Corresponding author. Mailing address: Department of Microbiology, BBRB 432/Box 8, 1530 3rd Avenue South, University of Alabama at Birmingham, Birmingham, AL 35294-2170. Phone: (205) 934-6593. Fax: (205) 954-5482. E-mail: dbedwell{at}uab.edu.

{dagger} Present address: Department of Systems Biology, Harvard Medical School, Boston, Mass.

{ddagger} Present address: Department of Biochemistry and Hillblom Center for the Biology of Aging, UCSF, San Francisco, Calif.

Molecular and Cellular Biology, July 2006, p. 5237-5248, Vol. 26, No. 14
0270-7306/06/$08.00+0     doi:10.1128/MCB.02448-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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