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Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein.

Centre National de la Recherche Scientifique, Laboratoire propre associé à Université Pierre et Marie Curie, Gif-sur-Yvette, France.

ABSTRACT

In Saccharomyces cerevisiae, temperature-sensitive mutations in the genes RNA14 and RNA15 correlate with a reduction of mRNA stability and poly(A) tail length. Although mRNA transcription is not abolished in these mutants, the transcripts are rapidly deadenylated as in a strain carrying an RNA polymerase B(II) temperature-sensitive mutation. This suggests that the primary defect could be in the control of the poly(A) status of the mRNAs and that the fast decay rate may be due to the loss of this control. By complementation of their temperature-sensitive phenotype, we have cloned the wild-type genes. They are essential for cell viability and are unique in the haploid genome. The RNA14 gene, located on chromosome H, is transcribed as three mRNAs, one major and two minor, which are 2.2, 1.5, and 1.1 kb in length. The RNA15 gene gives rise to a single 1.2-kb transcript and maps to chromosome XVI. Sequence analysis indicates that RNA14 encodes a 636-amino-acid protein with a calculated molecular weight of 75,295. No homology was found between RNA14 and RNA15 or between RNA14 and other proteins contained in data banks. The RNA15 DNA sequence predicts a protein of 296 amino acids with a molecular weight of 32,770. Sequence comparison reveals an N-terminal putative RNA-binding domain in the RNA15-encoded protein, followed by a glutamine and asparagine stretch similar to the opa sequences. Both RNA14 and RNA15 wild-type genes, when cloned on a multicopy plasmid, are able to suppress the temperature-sensitive phenotype of strains bearing either the rna14 or the rna15 mutation, suggesting that the encoded proteins could interact with each other.

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• Gross, S., Moore, C. L. (2001). Rna15 Interaction with the A-Rich Yeast Polyadenylation Signal Is an Essential Step in mRNA 3'-End Formation. Mol. Cell. Biol. 21: 8045-8055 [Abstract] [Full Text]  
• Tabb, M. M., Tongaonkar, P., Vu, L., Nomura, M. (2000). Evidence for Separable Functions of Srp1p, the Yeast Homolog of Importin alpha (Karyopherin alpha ): Role for Srp1p and Sts1p in Protein Degradation. Mol. Cell. Biol. 20: 6062-6073 [Abstract] [Full Text]  
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• McCarthy, J. E. G. (1998). Posttranscriptional Control of Gene Expression in Yeast. Microbiol. Mol. Biol. Rev. 62: 1492-1553 [Abstract] [Full Text]  
• Birse, C. E., Minvielle-Sebastia, L., Lee, B. A., Keller, W., Proudfoot, N. J. (1998). Coupling Termination of Transcription to Messenger RNA Maturation in Yeast. Science 280: 298-301 [Abstract] [Full Text]  
• Kessler, M. M., Henry, M. F., Shen, E., Zhao, J., Gross, S., Silver, P. A., Moore, C. L. (1997). Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3'-end formation in yeast. Genes Dev. 11: 2545-2556 [Abstract] [Full Text]  
• Barabino, S M, Hubner, W, Jenny, A, Minvielle-Sebastia, L, Keller, W (1997). The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins.. Genes Dev. 11: 1703-1716 [Abstract]  
• Kessler, M. M., Zhao, J., Moore, C. L. (1996). Purification of the Saccharomyces cerevisiae Cleavage/Polyadenylation Factor I. SEPARATION INTO TWO COMPONENTS THAT ARE REQUIRED FOR BOTH CLEAVAGE AND POLYADENYLATION OF mRNA 3prime ENDS. J. Biol. Chem. 271: 27167-27175 [Abstract] [Full Text]  
• Murthy, K G, Manley, J L (1995). The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation.. Genes Dev. 9: 2672-2683 [Abstract]  
• Singleton, D., Chen, S, Hitomi, M, Kumagai, C, Tartakoff, A. (1995). A yeast protein that bidirectionally affects nucleocytoplasmic transport. J. Cell Sci. 108: 265-272 [Abstract]  
• Minvielle-Sebastia, L, Preker, P., Keller, W (1994). RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor. Science 266: 1702-1705 [Abstract]  
• Bonneaud, N, Minvielle-Sebastia, L, Cullin, C, Lacroute, F (1994). Cellular localization of RNA14p and RNA15p, two yeast proteins involved in mRNA stability. J. Cell Sci. 107: 913-921 [Abstract]  
• Decker, C J, Parker, R (1993). A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation.. Genes Dev. 7: 1632-1643 [Abstract]  
• Mitchelson, A, Simonelig, M, Williams, C, O'Hare, K (1993). Homology with Saccharomyces cerevisiae RNA14 suggests that phenotypic suppression in Drosophila melanogaster by suppressor of forked occurs at the level of RNA stability.. Genes Dev. 7: 241-249 [Abstract]  
• Winstall, E., Sadowski, M., Kuhn, U., Wahle, E., Sachs, A. B. (2000). The Saccharomyces cerevisiae RNA-binding Protein Rbp29 Functions in Cytoplasmic mRNA Metabolism. J. Biol. Chem. 275: 21817-21826 [Abstract] [Full Text]  
• Gross, S., Moore, C. (2001). Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc. Natl. Acad. Sci. USA 98: 6080-6085 [Abstract] [Full Text]