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month download article/chapter yeast pre-mrna yeast mrna splicing 5-fluoro-orotic acid resistance yeast protein involved spt15 base editing ribosomal rna stability related subjects cold spring harbor wild-type gene full article pdf rna processing generates privacy choices/manage cookies mutations insts1 suppress thesaccharomyces cerevisiae rna14 rna-binding domain yeastcyc1 messenger rna thefip1 gene encodes mutation affecting stability thessm5-1 mutation restores intact yeast cells yeast sec23p acts prt1 protein subunit essential gene required polyadenylic acid sequences high efficiency transformation putative rrna helicase hanic-joyce pj european economic area scope submit manuscript inhibits dna synthesis apparent molecular weight high copy replicative coli shuttle vectors adenine-rich polymer retinoblastoma protein associates protein-protein interactions therna15-2 mutation present data suggest conditions privacy policy nucleic acids res thermosensitive mutant strainsrna15-2 messenger rnas western blot analysis sequence analysis reveals accepting optional cookies article molecular protein complex required yeastsec23 mutant allele hybrid system suggests

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• Jackson RJ, Standart N (1990) Does the poly(A) tail and 3′ untranslated region control mRNA translation?

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         headline:Mutations inSTS1 suppress the defect in 3′ mRNA processing caused by therna15-2 mutation inSaccharomyces cerevisiae
         description:In a search for proteins associated with Rna15p in processing the 3′ ends of messenger RNAs, we have looked for suppressors that correct, even partially, the thermosensitive growth defect of therna15-2 mutant. Mutations in a single locus that we namedSSM5, were able to suppress both the thermosensitivity of cell growth and the mRNA 3′ processing defect associated with therna15-2 mutation, but only slightly alleviated the thermosensitive growth defect of anrna14-1 mutant. Thessm5-1 mutant is sensitive to hydroxyurea at 37° C, a drug that inhibits DNA synthesis. By screening for complementation of the hydroxyurea-sensitive phenotype we cloned the corresponding wild-type gene and found that it corresponds to the essential geneSTS1 (also namedDBF8). Sts1p has an apparent molecular weight of 30 kDa and was confirmed to be a cytosolic protein by immunofluorescence analysis. Western blot analysis indicates that the thermosensitive mutant strainsrna15-2, rna14-1 andpap1-1 present a very low level of the Rna15p at 37° C. Thessm5-1 mutation restores the level of Rna15p in therna15-2 ssm5-1 double mutant. Use of the two-hybrid system suggests that Sts1p does not interact directly with Rna15p, but may be active as a homodimer. The present data suggest that Sts1p may play a role in the transport of Rna15p from the cytoplasm to the nucleus.
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      headline:Mutations inSTS1 suppress the defect in 3′ mRNA processing caused by therna15-2 mutation inSaccharomyces cerevisiae
      description:In a search for proteins associated with Rna15p in processing the 3′ ends of messenger RNAs, we have looked for suppressors that correct, even partially, the thermosensitive growth defect of therna15-2 mutant. Mutations in a single locus that we namedSSM5, were able to suppress both the thermosensitivity of cell growth and the mRNA 3′ processing defect associated with therna15-2 mutation, but only slightly alleviated the thermosensitive growth defect of anrna14-1 mutant. Thessm5-1 mutant is sensitive to hydroxyurea at 37° C, a drug that inhibits DNA synthesis. By screening for complementation of the hydroxyurea-sensitive phenotype we cloned the corresponding wild-type gene and found that it corresponds to the essential geneSTS1 (also namedDBF8). Sts1p has an apparent molecular weight of 30 kDa and was confirmed to be a cytosolic protein by immunofluorescence analysis. Western blot analysis indicates that the thermosensitive mutant strainsrna15-2, rna14-1 andpap1-1 present a very low level of the Rna15p at 37° C. Thessm5-1 mutation restores the level of Rna15p in therna15-2 ssm5-1 double mutant. Use of the two-hybrid system suggests that Sts1p does not interact directly with Rna15p, but may be active as a homodimer. The present data suggest that Sts1p may play a role in the transport of Rna15p from the cytoplasm to the nucleus.
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