Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Threonine-11, phosphorylated by Rad3 and atm in vitro, is required for activation of fission yeast checkpoint kinase Cds1

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Tanaka, K.
  • Boddy, Michael
  • Chen, X. B.
  • McGowan, C. H.
  • Russell, Paul

publication date

  • 2001

journal

  • Molecular and Cellular Biology  Journal

abstract

  • Fission yeast Cds1 is phosphorylated and activated when DNA replication is interrupted by nucleotide starvation or DNA damage. Cds1 enforces the S-M checkpoint that couples mitosis (M) to the completion of DNA synthesis (S). Cds1 also controls replicational stress tolerance mechanisms. Cds1 is regulated by a group of proteins that includes Rad3, a kinase related to human checkpoint kinase ATM (ataxia telangiectasia mutated). ATM phosphorylates serine or threonine followed by glutamine (SQ or TQ). Here we show that in vitro, Rad3 and ATM phosphorylate the N-terminal domain of Cds1 at the motif T(11)Q(12). Substitution of threonine-11 with alanine (T11A) abolished Cds1 activation that occurs when DNA replication is inhibited by hydroxyurea (HU) treatment. The cds1-T11A mutant was profoundly sensitive to HU, although not quite as sensitive as a cds1(-) null mutant. Cds1(T11A) was unable to enforce the S-M checkpoint. These results strongly suggest that Rad3-dependent phosphorylation of Cds1 at threonine-11 is required for Cds1 activation and function.

subject areas

  • Adenosine Triphosphatases
  • Checkpoint Kinase 2
  • DNA Helicases
  • Enzyme Activation
  • Phosphorylation
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces
  • Threonine
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.21.10.3398-3404.2001

PubMed ID

  • 11313465
scroll to property group menus

Additional Document Info

start page

  • 3398

end page

  • 3404

volume

  • 21

issue

  • 10

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support