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Cooperation of sumoylated chromosomal proteins in rDNA maintenance.

SUMO is a posttranslational modifier that can modulate protein activities, interactions, and localizations. As the GFP-Smt3p fusion protein has a preference for subnucleolar localization, especially when deconjugation is impaired, the nucleolar role of SUMO can be the key to its biological functions. Using conditional triple SUMO E3 mutants, we show that defects in sumoylation impair rDNA maintenance, i.e., the rDNA segregation is defective and the rDNA copy number decreases in these mutants. Upon characterization of sumoylated proteins involved in rDNA maintenance, we established that Top1p and Top2p, which are sumoylated by Siz1p/Siz2p, most likely collaborate with substrates of Mms21p to maintain rDNA integrity. Cohesin and condensin subunits, which both play important roles in rDNA stability and structures, are potential substrates of Mms21, as their sumoylation depends on Mms21p, but not Siz1p and Siz2p. In addition, binding of cohesin and condensin to rDNA is altered in the mms21-CH E3-deficient mutant.

Pubmed ID: 18846224

Authors

  • Takahashi Y
  • Dulev S
  • Liu X
  • Hiller NJ
  • Zhao X
  • Strunnikov A

Journal

PLoS genetics

Publication Data

October 10, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM080670
  • Agency: NIGMS NIH HHS, Id: R01 GM080670

Mesh Terms

  • Chromosomal Proteins, Non-Histone
  • DNA Topoisomerases
  • DNA, Fungal
  • DNA, Ribosomal
  • Genes, Fungal
  • Mutation
  • Nuclear Proteins
  • Protein Processing, Post-Translational
  • SUMO-1 Protein
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Ubiquitin-Protein Ligases