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Dosage suppressors of pds1 implicate ubiquitin-associated domains in checkpoint control

Academic Article
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Overview

authors

  • Clarke, D. J.
  • Mondesert, G.
  • Segal, M.
  • Bertolaet, B. L.
  • Jensen, S.
  • Wolff, M.
  • Henze, M.
  • Reed, Steven

publication date

  • March 2001

journal

  • Molecular and Cellular Biology  Journal

abstract

  • In budding yeast, anaphase initiation is controlled by ubiquitin-dependent degradation of Pds1p. Analysis of pds1 mutants implicated Pds1p in the DNA damage, spindle assembly, and S-phase checkpoints. Though some components of these pathways are known, others remain to be identified. Moreover, the essential function of Pds1p, independent of its role in checkpoint control, has not been elucidated. To identify loci that genetically interact with PDS1, we screened for dosage suppressors of a temperature-sensitive pds1 allele, pds1-128, defective for checkpoint control at the permissive temperature and essential for viability at 37 degrees C. Genetic and functional interactions of two suppressors are described. RAD23 and DDI1 suppress the temperature and hydroxyurea, but not radiation or nocodazole, sensitivity of pds1-128. rad23 and ddi1 mutants are partially defective in S-phase checkpoint control but are proficient in DNA damage and spindle assembly checkpoints. Therefore, Rad23p and Ddi1p participate in a subset of Pds1p-dependent cell cycle controls. Both Rad23p and Ddi1p contain ubiquitin-associated (UBA) domains which are required for dosage suppression of pds1-128. UBA domains are found in several proteins involved in ubiquitin-dependent proteolysis, though no function has been assigned to them. Deletion of the UBA domains of Rad23p and Ddi1p renders cells defective in S-phase checkpoint control, implicating UBA domains in checkpoint signaling. Since Pds1p destruction, and thus checkpoint regulation of mitosis, depends on ubiquitin-dependent proteolysis, we propose that the UBA domains functionally interact with the ubiquitin system to control Pds1p degradation in response to checkpoint activation.

subject areas

  • Amino Acid Sequence
  • Cell Cycle Proteins
  • Checkpoint Kinase 2
  • Fungal Proteins
  • Gamma Rays
  • Gene Dosage
  • Hydroxyurea
  • Molecular Sequence Data
  • Mutation
  • Nocodazole
  • Nuclear Proteins
  • Protein Kinases
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • S Phase
  • Saccharomyces cerevisiae Proteins
  • Securin
  • Suppression, Genetic
  • Ubiquitins
  • Yeasts
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Identity

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.21.6.1997-2007.2001

PubMed ID

  • 11238935
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Additional Document Info

start page

  • 1997

end page

  • 2007

volume

  • 21

issue

  • 6

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