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

DST1  -  Dst1p

Saccharomyces cerevisiae S288c

Synonyms: DNA strand transfer protein alpha, DNA strand transferase 1, PPR2, Pyrimidine pathway regulatory protein 2, STP-alpha, ...
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 DST1

  • The uninducible phenotype of this mutant is completely suppressed by an ochre suppressor, strengthening the hypothesis that PPR2 acts on URA4 transcription through the synthesis of a regulatory protein [1].
  • A regulatory gene PPR2 (pyrimidine pathway regulatory 2) acting specifically on this step, has been characterized, cloned and sequenced [1].
  • The short length of the PPR2 polypeptide chain and the presence of seven cysteine residues suggest that the active form of the protein is an oligomer assembled through disulphide bonds [1].
  • We found that the 6AU sensitivity of the rpo21 mutants can be suppressed by increasing the dosage of the wild-type PPR2 gene, presumably as a result of overexpression of TFIIS [2].
  • Deletion of PPR2 from the yeast genome is not lethal but renders cells sensitive to the uracil analog 6-azauracil (6AU) [2].

Biological context of DST1


Associations of DST1 with chemical compounds

  • In Saccharomyces cerevisiae, the gene encoding TFIIS (PPR2) is not essential, and disruption strains exhibit only mild phenotypes and an increased sensitivity to 6-azauracil [6].
  • Furthermore, we show that set2Delta ppr2Delta double mutants (PPR2 encodes TFIIS, a transcription elongation factor) are synthetically hypersensitive to 6-azauracil, and that deletions in the CTD reduce in vivo levels of H3 lysine 36 methylation [7].

Regulatory relationships of DST1


Other interactions of DST1

  • Disruptions of PPR2 are lethal in conjunction with a disruption in the nonessential gene TAF14/TFG3 [8].
  • This led to the finding that Ess1 also inhibits elongation; Ess1 opposes elongation factors Dst1 and Spt4/5, and overexpression of ESS1 makes cells more sensitive to the elongation inhibitor 6-AU [9].
  • Moreover, the synthetic interactions of these mutants with soh1, spt4, and dst1 suggest differential in vivo effects [10].
  • One region D substitution is lethal unless suppressed by a substitution in region G and interacts genetically with PPR2, the gene encoding transcription elongation factor IIS [11].
  • Here we demonstrate that deletion of the CTK1 gene, encoding the kinase subunit of RNA polymerase II carboxy-terminal domain kinase I (CTDK-I), is synthetically lethal when combined with deletion of PPR2 or ELP genes [12].


  1. Complete sequence of a eukaryotic regulatory gene. Hubert, J.C., Guyonvarch, A., Kammerer, B., Exinger, F., Liljelund, P., Lacroute, F. EMBO J. (1983) [Pubmed]
  2. Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II. Archambault, J., Lacroute, F., Ruet, A., Friesen, J.D. Mol. Cell. Biol. (1992) [Pubmed]
  3. Isolation, DNA sequence, and regulation of a Saccharomyces cerevisiae gene that encodes DNA strand transfer protein alpha. Clark, A.B., Dykstra, C.C., Sugino, A. Mol. Cell. Biol. (1991) [Pubmed]
  4. Genetic interactions of DST1 in Saccharomyces cerevisiae suggest a role of TFIIS in the initiation-elongation transition. Malagon, F., Tong, A.H., Shafer, B.K., Strathern, J.N. Genetics (2004) [Pubmed]
  5. Cloning and characterization of DST2, the gene for DNA strand transfer protein beta from Saccharomyces cerevisiae. Dykstra, C.C., Kitada, K., Clark, A.B., Hamatake, R.K., Sugino, A. Mol. Cell. Biol. (1991) [Pubmed]
  6. Genetic interactions between TFIIS and the Swi-Snf chromatin-remodeling complex. Davie, J.K., Kane, C.M. Mol. Cell. Biol. (2000) [Pubmed]
  7. The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II. Li, B., Howe, L., Anderson, S., Yates, J.R., Workman, J.L. J. Biol. Chem. (2003) [Pubmed]
  8. Genetic interactions between TFIIF and TFIIS. Fish, R.N., Ammerman, M.L., Davie, J.K., Lu, B.F., Pham, C., Howe, L., Ponticelli, A.S., Kane, C.M. Genetics (2006) [Pubmed]
  9. The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae. Wu, X., Rossettini, A., Hanes, S.D. Genetics (2003) [Pubmed]
  10. Mutations in the Saccharomyces cerevisiae RPB1 Gene Conferring Hypersensitivity to 6-Azauracil. Malagon, F., Kireeva, M.L., Shafer, B.K., Lubkowska, L., Kashlev, M., Strathern, J.N. Genetics (2006) [Pubmed]
  11. Stimulation of transcription by mutations affecting conserved regions of RNA polymerase II. Archambault, J., Jansma, D.B., Kawasoe, J.H., Arndt, K.T., Greenblatt, J., Friesen, J.D. J. Bacteriol. (1998) [Pubmed]
  12. Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo. Jona, G., Wittschieben, B.O., Svejstrup, J.Q., Gileadi, O. Gene (2001) [Pubmed]
WikiGenes - Universities