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Gene Review

UBP10  -  Ubp10p

Saccharomyces cerevisiae S288c

Synonyms: DOT4, Deubiquitinating enzyme 10, Disrupter of telomere silencing protein 4, N1619, Ubiquitin carboxyl-terminal hydrolase 10, ...
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High impact information on UBP10

  • We compare Ubp10 to Ubp8, the SAGA-associated H2B deubiquitylase involved in gene activation, and show that telomeric and gene-silencing functions are specific to Ubp10 [1].
  • Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing [1].
  • Ubp10 is also localized to the rDNA locus, a second silenced domain, where it similarly maintains low histone methylation [1].
  • Consistent with its role in silencing, Ubp10p is preferentially localized to silent chromatin where its ubiquitin protease activity maintains low levels of H3 Lys4 and Lys79 methylation to allow optimal Sir protein binding to telomeres and global telomeric silencing [2].
  • Together, these findings suggest that Dot4p regulates silencing by acting on Sir4p [3].

Biological context of UBP10

  • DOT4 links silencing and cell growth in Saccharomyces cerevisiae [3].
  • UBP10 codes for a deubiquitinating enzyme of Saccharomyces cerevisiae whose loss of function determines slow growth rate and partial impairment of silencing at telomeres and HM loci [4].
  • All these results argue in favour of an involvement of the yeast metacaspase in the active cell death triggered by loss of UBP10 function [5].
  • A genome-wide analysis performed on a ubp10 disruptant revealed alterations in expression of subtelomeric genes together with a broad change in the whole transcriptional profile, closely parallel to that induced by oxidative stress [4].
  • Here, we show that additional deletion of YCA1, coding for the yeast metacaspase, suppressed the ubp10 disruptant phenotype [5].

Physical interactions of UBP10

  • By two-hybrid analysis, the amino-terminal third of Dot4p interacts with the silencing protein Sir4p [3].

Regulatory relationships of UBP10

  • We conclude that Dot4p is involved in posttranscriptionally regulating Gap1p, and possibly other transporters as well [6].

Other interactions of UBP10

  • Cells lacking DOT4 exhibited reduced silencing and a corresponding decrease in the level of Sir4p [3].
  • DOT4 encodes an ubiquitin processing protease (hydrolase) that is primarily located in the nucleus [3].
  • We also show that the activity of the amino acid permease Gap1p is reduced in DOT4 mutants [6].
  • Moreover, deletion of the latter two genes weakened silencing as well, suggesting that DOT1 and DOT4 normally play important roles in gene repression [7].


  1. Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing. Emre, N.C., Ingvarsdottir, K., Wyce, A., Wood, A., Krogan, N.J., Henry, K.W., Li, K., Marmorstein, R., Greenblatt, J.F., Shilatifard, A., Berger, S.L. Mol. Cell (2005) [Pubmed]
  2. Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin. Gardner, R.G., Nelson, Z.W., Gottschling, D.E. Mol. Cell. Biol. (2005) [Pubmed]
  3. DOT4 links silencing and cell growth in Saccharomyces cerevisiae. Kahana, A., Gottschling, D.E. Mol. Cell. Biol. (1999) [Pubmed]
  4. Transcriptional profiling of ubp10 null mutant reveals altered subtelomeric gene expression and insurgence of oxidative stress response. Orlandi, I., Bettiga, M., Alberghina, L., Vai, M. J. Biol. Chem. (2004) [Pubmed]
  5. Involvement of the yeast metacaspase Yca1 in ubp10Delta-programmed cell death. Bettiga, M., Calzari, L., Orlandi, I., Alberghina, L., Vai, M. FEMS Yeast Res. (2004) [Pubmed]
  6. The deubiquitinating enzyme Dot4p is involved in regulating nutrient uptake. Kahana, A. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  7. Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae. Singer, M.S., Kahana, A., Wolf, A.J., Meisinger, L.L., Peterson, S.E., Goggin, C., Mahowald, M., Gottschling, D.E. Genetics (1998) [Pubmed]
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