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A novel role of the N terminus of budding yeast histone H3 variant Cse4 in ubiquitin-mediated proteolysis.

Regulating levels of centromeric histone H3 (CenH3) variant is crucial for genome stability. Interaction of Psh1, an E3 ligase, with the C terminus of Cse4 has been shown to contribute to its proteolysis. Here, we demonstrate a role for ubiquitination of the N terminus of Cse4 in regulating Cse4 proteolysis for faithful chromosome segregation and a role for Doa1 in ubiquitination of Cse4.

Pubmed ID: 23525333

Authors

  • Au WC
  • Dawson AR
  • Rawson DW
  • Taylor SB
  • Baker RE
  • Basrai MA

Journal

Genetics

Publication Data

June 4, 2013

Associated Grants

  • Agency: Intramural NIH HHS, Id:

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Chromosomal Proteins, Non-Histone
  • Chromosome Segregation
  • DNA-Binding Proteins
  • Mutation
  • Protein Structure, Tertiary
  • Proteolysis
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitination