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Gene Review

RNA15  -  Rna15p

Saccharomyces cerevisiae S288c

Synonyms: YGL044C, mRNA 3'-end-processing protein RNA15
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High impact information on RNA15

  • RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor [1].
  • By this approach, we have identified a RNAP II termination domain in the well-defined cleavage polyadenylation factor called CstF-64 in metazoans and Rna15p in S. cerevisiae [2].
  • We described previously an unexpected association between a transcription factor, PC4 (or Sub1 in yeast), and an mRNA polyadenylation factor, CstF-64 (Rna15 in yeast), and provided evidence that this was important for efficient transcription elongation [3].
  • Furthermore, a quantitative analysis of transcription run-on performed on temperature-sensitive mutant strains reveals that the lack of either functional Rna14p or Pcf11p affects transcription termination more severely than the absence of a functional Rna15p [4].
  • However, in complex with Hrp1 and Rna14, Rna15 specifically interacts with the A-rich element [5].

Biological context of RNA15


Associations of RNA15 with chemical compounds

  • 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 [7].

Physical interactions of RNA15

  • Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro [8].
  • The present data suggest that Sts1p may play a role in the transport of Rna15p from the cytoplasm to the nucleus [9].

Other interactions of RNA15

  • We observed that the rates of deadenylation are not affected by lesions in either the RNA14 or the RNA15 gene [6].
  • Moreover, fractions obtained by anion-exchange chromatography of extracts from the wild-type strain contain both Pcf11 and Rna15 in the same fractions, as shown by immunoblotting with a Pcf11-specific antibody [10].
  • These observations suggest that the RNA14, RNA15, and PAP1 proteins are involved in poly(A) site choice [6].
  • The Pcf11-2 thermosensitive strain shows a shortening of the poly(A) tails and a strong decrease in the steady-state level of actin transcripts after a shift to the nonpermissive temperature as do the thermosensitive alleles of RNA14 and RNA15 [10].
  • One of these is the previously known RNA15, which, like NPL3, also encodes a protein with similarity to the vertebrate hnRNP A/B protein family [11].

Analytical, diagnostic and therapeutic context of RNA15


  1. RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor. Minvielle-Sebastia, L., Preker, P.J., Keller, W. Science (1994) [Pubmed]
  2. Transcriptional termination factors for RNA polymerase II in yeast. Aranda, A., Proudfoot, N. Mol. Cell (2001) [Pubmed]
  3. The transcriptional coactivator PC4/Sub1 has multiple functions in RNA polymerase II transcription. Calvo, O., Manley, J.L. EMBO J. (2005) [Pubmed]
  4. Cleavage/polyadenylation factor IA associates with the carboxyl-terminal domain of RNA polymerase II in Saccharomyces cerevisiae. Barillà, D., Lee, B.A., Proudfoot, N.J. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  5. Rna15 interaction with the A-rich yeast polyadenylation signal is an essential step in mRNA 3'-end formation. Gross, S., Moore, C.L. Mol. Cell. Biol. (2001) [Pubmed]
  6. Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo. Mandart, E., Parker, R. Mol. Cell. Biol. (1995) [Pubmed]
  7. 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. Minvielle-Sebastia, L., Winsor, B., Bonneaud, N., Lacroute, F. Mol. Cell. Biol. (1991) [Pubmed]
  8. Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro. Amrani, N., Minet, M., Le Gouar, M., Lacroute, F., Wyers, F. Mol. Cell. Biol. (1997) [Pubmed]
  9. Mutations in STS1 suppress the defect in 3' mRNA processing caused by the rna15-2 mutation in Saccharomyces cerevisiae. Amrani, N., Dufour, M.E., Bonneaud, N., Lacroute, F. Mol. Gen. Genet. (1996) [Pubmed]
  10. PCF11 encodes a third protein component of yeast cleavage and polyadenylation factor I. Amrani, N., Minet, M., Wyers, F., Dufour, M.E., Aggerbeck, L.P., Lacroute, F. Mol. Cell. Biol. (1997) [Pubmed]
  11. Potential RNA binding proteins in Saccharomyces cerevisiae identified as suppressors of temperature-sensitive mutations in NPL3. Henry, M., Borland, C.Z., Bossie, M., Silver, P.A. Genetics (1996) [Pubmed]
  12. Cellular localization of RNA14p and RNA15p, two yeast proteins involved in mRNA stability. Bonneaud, N., Minvielle-Sebastia, L., Cullin, C., Lacroute, F. J. Cell. Sci. (1994) [Pubmed]
  13. Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins. Cullin, C., Minvielle-Sebastia, L. Yeast (1994) [Pubmed]
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