Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint.
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.
Sun
Z
Z
Department of Biology, Yale University, New Haven, CT 06511, USA.
Hsiao
J
J
Fay
D S
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Stern
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D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins; D064447:Checkpoint Kinase 2; D004249:DNA Damage; D004261:DNA Replication / Q000187:drug effects; D005656:Fungal Proteins / Q000378:metabolism*; D016195:G2 Phase; D006918:Hydroxyurea / Q000494:pharmacology; D008741:Methyl Methanesulfonate / Q000494:pharmacology; D008938:Mitosis; D009154:Mutation; D009842:Oligopeptides; D010455:Peptides; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D014158:Transcription, Genetic
D018797:Cell Cycle Proteins; D005656:Fungal Proteins; D009842:Oligopeptides; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; C069930:rad9 protein; C085706:FLAG peptide; D008741:Methyl Methanesulfonate; D011494:Protein Kinases; D064447:Checkpoint Kinase 2; D017346:Protein Serine-Threonine Kinases; C067022:RAD53 protein, S cerevisiae; D006918:Hydroxyurea