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Gene Review

DDI1  -  Ddi1p

Saccharomyces cerevisiae S288c

Synonyms: DNA damage-inducible protein 1, VSM1, YER143W, v-SNARE-master 1
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High impact information on DDI1

  • RAD23 and DDI1 suppress the temperature and hydroxyurea, but not radiation or nocodazole, sensitivity of pds1-128. rad23 and ddi1 mutants are partially defective in S-phase checkpoint control but are proficient in DNA damage and spindle assembly checkpoints [1].
  • On the basis of these results, we propose that Vsm1 is a novel v-SNARE-interacting protein that appears to act as negative regulator of constitutive exocytosis [2].
  • Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis [2].
  • Importantly, Vsm1 binding to Sso seems to preclude Sso binding to its partner t-SNARE, Sec9, and vice versa [3].
  • Phosphorylation of Sso increases its affinity for Vsm1 by more than fivefold in vitro and both phosphorylated Sso1, as well as Sso1 bearing an aspartate substitution at position 79, interact tightly with Vsm1 [3].

Biological context of DDI1


Associations of DDI1 with chemical compounds

  • Furthermore, MAG1 and DDI1 respond differently in the presence of the protein synthesis inhibitor cycloheximide, suggesting that these two genes are regulated by different mechanisms in the absence of de novo protein synthesis [7].
  • The substitution of serine-79 in Sso1 with an alanine residue or the treatment of yeast with C2-ceramide, which results in the dephosphorylation of serine-79, both inhibit Vsm1 binding in vivo [3].
  • Vsm1 binding is dependent upon the NH2-terminal autoinhibitory domain of Sso, and constitutively "open" forms of the t-SNARE show a reduction in Vsm1 binding in vivo [3].

Other interactions of DDI1

  • The Saccharomyces cerevisiae genes RAD23 and DDI1 were identified in a screen for multicopy suppressors of the temperature-sensitivity of a mutant allele of S. cerevisiae PDS1 [8].
  • In order to understand how damage checkpoints control the expression of DNA damage-inducible genes, the transcript level of two closely clustered genes, MAG1 and DDI1, was examined in a number of checkpoint mutants [4].
  • Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-directional promoter element [9].


  1. Dosage suppressors of pds1 implicate ubiquitin-associated domains in checkpoint control. Clarke, D.J., Mondesert, G., Segal, M., Bertolaet, B.L., Jensen, S., Wolff, M., Henze, M., Reed, S.I. Mol. Cell. Biol. (2001) [Pubmed]
  2. Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis. Lustgarten, V., Gerst, J.E. Mol. Cell. Biol. (1999) [Pubmed]
  3. Phosphorylation of the autoinhibitory domain of the Sso t-SNAREs promotes binding of the Vsm1 SNARE regulator in yeast. Marash, M., Gerst, J.E. Mol. Biol. Cell (2003) [Pubmed]
  4. Two alternative cell cycle checkpoint pathways differentially control DNA damage-dependent induction of MAG1 and DDI1 expression in yeast. Zhu, Y., Xiao, W. Mol. Genet. Genomics (2001) [Pubmed]
  5. Differential regulation of two closely clustered yeast genes, MAG1 and DDI1, by cell-cycle checkpoints. Zhu, Y., Xiao, W. Nucleic Acids Res. (1998) [Pubmed]
  6. Bidirectional regulation of two DNA-damage-inducible genes, MAG1 and DDI1, from Saccharomyces cerevisiae. Liu, Y., Xiao, W. Mol. Microbiol. (1997) [Pubmed]
  7. UAS(MAG1), a yeast cis-acting element that regulates the expression of MAG1, is located within the protein coding region of DDI1. Liu, Y., Dai, H., Xiao, W. Mol. Gen. Genet. (1997) [Pubmed]
  8. UBA domains mediate protein-protein interactions between two DNA damage-inducible proteins. Bertolaet, B.L., Clarke, D.J., Wolff, M., Watson, M.H., Henze, M., Divita, G., Reed, S.I. J. Mol. Biol. (2001) [Pubmed]
  9. Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-directional promoter element. Zhu, Y., Xiao, W. Nucleic Acids Res. (2004) [Pubmed]
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