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Gene Review

SIZ1  -  SUMO ligase SIZ1

Saccharomyces cerevisiae S288c

Synonyms: E3 SUMO-protein ligase SIZ1, SAP and Miz-finger domain-containing protein 1, ULL1, Ubiquitin-like protein ligase 1, YDR409W
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Disease relevance of SIZ1

  • Mutant siz1 plants exhibit constitutive systemic-acquired resistance (SAR) characterized by elevated accumulation of salicylic acid (SA), increased expression of pathogenesis-related (PR) genes, and increased resistance to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000 [1].

High impact information on SIZ1

  • Siz1 is required for SUMO attachment to the S. cerevisiae septins in vivo and strongly stimulates septin sumoylation in vitro [2].
  • Siz1 and the related protein Siz2 promote SUMO conjugation to different substrates at different stages of the cell cycle and, together, are required for most SUMO conjugation in yeast [2].
  • Lastly, we demonstrate that selection of proper DNA repair pathways to stalled DNA replication forks is controlled by the Mec1-dependent checkpoint and is executed by cooperative functions of Siz1 and Srs2 [3].
  • However, yeast mutants lacking the SUMO ligases Siz1 and Siz2/Nfi1 are viable, even though they show dramatically reduced levels of SUMO conjugation [4].
  • Most informatively, mutants lacking the SUMO E3 ligase Siz1 are strongly doxorubicin resistant, whereas mutants of other SUMO ligases are either weakly resistant (siz2) or hypersensitive (mms21) to doxorubicin [5].

Biological context of SIZ1


Associations of SIZ1 with chemical compounds


Other interactions of SIZ1

  • The previously uncharacterized SIZ1 (SAP and Miz) gene, which encodes a protein containing a predicted DNA-binding SAP module and a Miz finger, is identified as a bypass suppressor of the growth defect associated with the SMT4 disruption [6].
  • Recently, Ull1/Siz1 was discovered as a novel PIAS-type E3 required for septin sumoylation in yeast [8].
  • Siz1 is a member of a new family (Miz1, PIAS3, etc.) containing a conserved domain with a similarity to a zinc-binding RING-domain, often found in ubiquitin ligases [7].


  1. Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase. Lee, J., Nam, J., Park, H.C., Na, G., Miura, K., Jin, J.B., Yoo, C.Y., Baek, D., Kim, D.H., Jeong, J.C., Kim, D., Lee, S.Y., Salt, D.E., Mengiste, T., Gong, Q., Ma, S., Bohnert, H.J., Kwak, S.S., Bressan, R.A., Hasegawa, P.M., Yun, D.J. Plant J. (2007) [Pubmed]
  2. An E3-like factor that promotes SUMO conjugation to the yeast septins. Johnson, E.S., Gupta, A.A. Cell (2001) [Pubmed]
  3. Regulation of gross chromosomal rearrangements by ubiquitin and SUMO ligases in Saccharomyces cerevisiae. Motegi, A., Kuntz, K., Majeed, A., Smith, S., Myung, K. Mol. Cell. Biol. (2006) [Pubmed]
  4. Misregulation of 2 microm circle copy number in a SUMO pathway mutant. Chen, X.L., Reindle, A., Johnson, E.S. Mol. Cell. Biol. (2005) [Pubmed]
  5. Small ubiquitin-related modifier pathway is a major determinant of doxorubicin cytotoxicity in Saccharomyces cerevisiae. Huang, R.Y., Kowalski, D., Minderman, H., Gandhi, N., Johnson, E.S. Cancer Res. (2007) [Pubmed]
  6. Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation. Strunnikov, A.V., Aravind, L., Koonin, E.V. Genetics (2001) [Pubmed]
  7. A novel factor required for the SUMO1/Smt3 conjugation of yeast septins. Takahashi, Y., Toh-e, A., Kikuchi, Y. Gene (2001) [Pubmed]
  8. Comparative analysis of yeast PIAS-type SUMO ligases in vivo and in vitro. Takahashi, Y., Toh-E, A., Kikuchi, Y. J. Biochem. (2003) [Pubmed]
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