Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint

Science  10 Jul 1998:
Vol. 281, Issue 5374, pp. 272-274
DOI: 10.1126/science.281.5374.272

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The Rad53 protein kinase of Saccharomyces cerevisiae is required for checkpoints that prevent cell division in cells with damaged or incompletely replicated DNA. The Rad9 protein was phosphorylated in response to DNA damage, and phosphorylated Rad9 interacted with the COOH-terminal forkhead homology–associated (FHA) domain of Rad53. Inactivation of this domain abolished DNA damage–dependent Rad53 phosphorylation, G2/M cell cycle phase arrest, and increase of RNR3 transcription but did not affect replication inhibition–dependent Rad53 phosphorylation. Thus, Rad53 integrates DNA damage signals by coupling with phosphorylated Rad9. The hitherto uncharacterized FHA domain appears to be a modular protein-binding domain.

  • * Present address: Room B058, Porter Biosciences, MCD Biology, University of Colorado, Boulder, CO 80309–0347, USA.

  • To whom correspondence should be addressed. E-mail: Stern{at}

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