Centromere binding and a conserved role in chromosome stability for SUMO-dependent ubiquitin ligases

PLoS One. 2013 Jun 13;8(6):e65628. doi: 10.1371/journal.pone.0065628. Print 2013.

Abstract

The Saccharomyces cerevisiae Slx5/8 complex is the founding member of a recently defined class of SUMO-targeted ubiquitin ligases (STUbLs). Slx5/8 has been implicated in genome stability and transcription, but the precise contribution is unclear. To characterise Slx5/8 function, we determined genome-wide changes in gene expression upon loss of either subunit. The majority of mRNA changes are part of a general stress response, also exhibited by mutants of other genome integrity pathways and therefore indicative of an indirect effect on transcription. Genome-wide binding analysis reveals a uniquely centromeric location for Slx5. Detailed phenotype analyses of slx5Δ and slx8Δ mutants show severe mitotic defects that include aneuploidy, spindle mispositioning, fish hooks and aberrant spindle kinetics. This is associated with accumulation of the PP2A regulatory subunit Rts1 at centromeres prior to entry into anaphase. Knockdown of the human STUbL orthologue RNF4 also results in chromosome segregation errors due to chromosome bridges. The study shows that STUbLs have a conserved role in maintenance of chromosome stability and links SUMO-dependent ubiquitination to a centromere-specific function during mitosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aneuploidy
  • Centromere / genetics
  • Centromere / metabolism*
  • Chromosomal Instability*
  • Chromosome Mapping
  • Gene Deletion
  • Genome, Fungal
  • Genomic Instability
  • Metaphase
  • Mutation
  • Phenotype
  • Plasmids / genetics
  • Protein Binding
  • Protein Phosphatase 2 / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Small Ubiquitin-Related Modifier Proteins / metabolism*
  • Spindle Apparatus / metabolism
  • Stress, Physiological
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism*

Substances

  • Saccharomyces cerevisiae Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Slx8 protein, S cerevisiae
  • Ubiquitin-Protein Ligases
  • Protein Phosphatase 2
  • Rts1 protein, S cerevisiae
  • Slx5 protein, S cerevisiae

Grants and funding

This work was funded by the Netherlands Bioinformatics Centre (NBIC) and the Netherlands Organization of Scientific Research (NWO), grants 016.108.607, 817.02.015, 050.71.057, 911.06.009. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.