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Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint
Author(s): Sun ZX, Hsiao J, Fay DS, Stern DF
Source: SCIENCE    Volume: 281    Issue: 5374    Pages: 272-274    Published: JUL 10 1998  
Times Cited: 244     References: 30     
Abstract: 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, G(2)/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.
Document Type: Article
Language: English
Reprint Address: Stern, DF (reprint author), Yale Univ, Sch Med, Dept Pathol, 310 Cedar St,Room BML 342, New Haven, CT 06520 USA
Addresses:
1. Yale Univ, Sch Med, Dept Pathol, New Haven, CT 06520 USA
2. Yale Univ, Dept Biol, New Haven, CT 06511 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: ZZ286
ISSN: 0036-8075
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