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

• Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo [5].
• In Saccharomyces cerevisiae, temperature-sensitive mutations in the genes RNA14 and RNA15 correlate with a reduction of mRNA stability and poly(A) tail length [6].
• 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 [6].
• Surprisingly, the RNA14 promoter itself is not essential for this phenotype of the rna14-5 mutant [7].

Anatomical context of RNA14

• Rna14p, a component of the yeast nuclear cleavage/polyadenylation factor I, is also localised in mitochondria [8].

Regulatory relationships of RNA14

• Disruption of the SSM4 gene does not affect cell viability and suppresses the rna14 mutant phenotypes [9].

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].

References