The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RNA14  -  Rna14p

Saccharomyces cerevisiae S288c

Synonyms: YM9796.14, YMR061W, mRNA 3'-end-processing protein RNA14
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on RNA14

  • Coimmunoprecipitation experiments reveal that RNA14, a subunit of cleavage factor I (CF I), directly interacts with FIP1, but not with PAP1 [1].
  • RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor [2].
  • Here, mutations in the PAP1 gene were shown to be synergistically lethal with previously identified mutations in the RNA14 and RNA15 genes, which suggests that their encoded proteins participate in 3'-end processing [2].
  • The major predicted gene product is an 84- kD protein that is homologous to RNA14 of Saccharomyces cerevisiae, a vital gene where mutation affects mRNA stability [3].
  • First by affinity chromatography experiments with yeast extracts we demonstrate that the Rna15p, Rna14p, and Pcf11p subunits of this complex are associated with phosphorylated CTD [4].

Biological context of RNA14


Anatomical context of RNA14


Regulatory relationships of RNA14


Other interactions of RNA14

  • We observed that the rates of deadenylation are not affected by lesions in either the RNA14 or the RNA15 gene [5].
  • These observations suggest that the RNA14, RNA15, and PAP1 proteins are involved in poly(A) site choice [5].
  • Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to rna14 mutations [9].
  • The Rna14-Rna15 complex, unlike the individual components, binds to an RNA oligonucleotide derived from the 3'-untranslated region of the S.cerevisiae GAL7 gene [10].

Analytical, diagnostic and therapeutic context of RNA14

  • Sequence analysis indicates that RNA14 encodes a 636-amino-acid protein with a calculated molecular weight of 75,295 [6].
  • We have raised antibodies to the RNA14 and RNA15 proteins, and used subcellular fractionation and immunofluorescence to localize these proteins within the yeast cell [11].
  • Site-directed mutagenesis experiments provided additional data suggesting that the rna14-5 mutation acts at the protein level rather than modifying the properties of the RNA14 transcripts themselves [7].
  • Analytical ultracentrifugation reveals that Rna14 mediates this association and facilitates assembly of an A2B2 tetramer (M(r) 230 000), where relatively compact Rna14-Rna15 heterodimers are in rapid equilibrium with tetramers that have a more extended shape [10].


  1. The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase. Preker, P.J., Lingner, J., Minvielle-Sebastia, L., Keller, W. Cell (1995) [Pubmed]
  2. 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]
  3. Homology with Saccharomyces cerevisiae RNA14 suggests that phenotypic suppression in Drosophila melanogaster by suppressor of forked occurs at the level of RNA stability. Mitchelson, A., Simonelig, M., Williams, C., O'Hare, K. Genes Dev. (1993) [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. 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]
  6. 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]
  7. Expression analysis of RNA14, a gene involved in mRNA 3' end maturation in yeast: characterization of the rna14-5 mutant strain. Brendolise, C., Rouillard, J.M., Dufour, M.E., Lacroute, F. Mol. Genet. Genomics (2002) [Pubmed]
  8. Rna14p, a component of the yeast nuclear cleavage/polyadenylation factor I, is also localised in mitochondria. Rouillard, J.M., Brendolise, C., Lacroute, F. Mol. Gen. Genet. (2000) [Pubmed]
  9. Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to rna14 mutations. Mandart, E., Dufour, M.E., Lacroute, F. Mol. Gen. Genet. (1994) [Pubmed]
  10. Rna14-Rna15 assembly mediates the RNA-binding capability of Saccharomyces cerevisiae cleavage factor IA. Noble, C.G., Walker, P.A., Calder, L.J., Taylor, I.A. Nucleic Acids Res. (2004) [Pubmed]
  11. 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]
WikiGenes - Universities