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Gene Review

UBP8  -  Ubp8p

Saccharomyces cerevisiae S288c

Synonyms: Deubiquitinating enzyme 8, Ubiquitin carboxyl-terminal hydrolase 8, Ubiquitin thioesterase 8, Ubiquitin-specific-processing protease 8, YM9959.05, ...
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High impact information on UBP8

  • Deletion of Ubp8 lowered transcription of SAGA-regulated genes, and the severity of this defect was exacerbated by codeletion of the Gcn5 acetyltransferase within SAGA [1].
  • We show that Ubp8, a component of the SAGA acetylation complex, is required for SAGA-mediated deubiquitylation of histone H2B in vitro [1].
  • In addition, disruption of either ubiquitylation or Ubp8-mediated deubiquitylation of H2B resulted in altered levels of gene-associated H3 Lys 4 methylation and Lys 36 methylation, which have both been linked to transcription [1].
  • Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8 [1].
  • 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 [2].

Biological context of UBP8

  • Like that at GAL1, H3-K4 methylation is increased at the PHO84 core promoter in the UBP8 deletion mutant [3].
  • Using mutagenesis, we identified a putative zinc (Zn) binding domain within Ubp8 as being critical for the association with SAGA [4].

Associations of UBP8 with chemical compounds

  • Furthermore, trimethylation of H3 at lysine 4 within the UAS increases significantly under activating conditions, and remarkably, Ubp8 is shown to have a role in regulating the methylation status of this residue [5].

Other interactions of UBP8

  • SAGA purified from a sgf11 Delta deletion strain has reduced amounts of Ubp8p, and a ubp8 Delta deletion strain shows changes in transcription similar to those seen with the sgf11 Delta deletion strain [6].
  • SAGA combines proteins involved in interactions with DNA-bound activators and TATA-binding protein (TBP), as well as enzymes for histone acetylation (Gcn5) and histone deubiquitylation (Ubp8) [4].
  • The recent finding that the removal of the ubiquitin group from H2B is performed by a component of SAGA, Ubp8, is intriguing as it assigns two posttranslation modification processes to one complex [7].
  • Here we show that a putative deubiquitinating enzyme, Ubp8, is a structurally nonessential component of both the Spt-Ada-Gcn5-acetyltransferase (SAGA) and SAGA-like (SLIK) histone acetyltransferase (HAT) complexes in yeast [5].


  1. Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Henry, K.W., Wyce, A., Lo, W.S., Duggan, L.J., Emre, N.C., Kao, C.F., Pillus, L., Shilatifard, A., Osley, M.A., Berger, S.L. Genes Dev. (2003) [Pubmed]
  2. 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]
  3. Ubp8p, a histone deubiquitinase whose association with SAGA is mediated by Sgf11p, differentially regulates lysine 4 methylation of histone H3 in vivo. Shukla, A., Stanojevic, N., Duan, Z., Sen, P., Bhaumik, S.R. Mol. Cell. Biol. (2006) [Pubmed]
  4. H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex. Ingvarsdottir, K., Krogan, N.J., Emre, N.C., Wyce, A., Thompson, N.J., Emili, A., Hughes, T.R., Greenblatt, J.F., Berger, S.L. Mol. Cell. Biol. (2005) [Pubmed]
  5. Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription. Daniel, J.A., Torok, M.S., Sun, Z.W., Schieltz, D., Allis, C.D., Yates, J.R., Grant, P.A. J. Biol. Chem. (2004) [Pubmed]
  6. Cluster analysis of mass spectrometry data reveals a novel component of SAGA. Powell, D.W., Weaver, C.M., Jennings, J.L., McAfee, K.J., He, Y., Weil, P.A., Link, A.J. Mol. Cell. Biol. (2004) [Pubmed]
  7. The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex. Lee, K.K., Florens, L., Swanson, S.K., Washburn, M.P., Workman, J.L. Mol. Cell. Biol. (2005) [Pubmed]
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