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

• Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo [6].
• In Saccharomyces cerevisiae, temperature-sensitive mutations in the genes RNA14 and RNA15 correlate with a reduction of mRNA stability and poly(A) tail length [7].
• The RNA15 gene gives rise to a single 1.2-kb transcript and maps to chromosome XVI [7].
• The RNA15 DNA sequence predicts a protein of 296 amino acids with a molecular weight of 32,770 [7].

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

• 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 [7].
• We have raised antibodies to the RNA14 and RNA15 proteins, and used subcellular fractionation and immunofluorescence to localize these proteins within the yeast cell [12].
• We found that Pab1 interacts with Rna15 in two-hybrid assays and in coimmunoprecipitation experiments [8].
• Here, we present results showing the functional expression and the efficient immunoprecipitation of the epitope-tagged Rna15 protein, which is involved in Saccharomyces cerevisiae mRNA stability [13].
• Western blot analysis indicates that the thermosensitive mutant strains rna15-2, rna14-1 and pap1-1 present a very low level of the Rna15p at 37 degrees C. The ssm5-1 mutation restores the level of Rna15p in the rna15-2 ssm5-1 double mutant [9].

References