Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint
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- Zhaoxia Sun
- Z. Sun, Department of Biology, Yale University, New Haven, CT 06511, USA, and Department of Pathology, Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA. J. Hsiao, D. S. Fay, D. F. Stern, Department of Pathology,Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA.
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- James Hsiao
- Z. Sun, Department of Biology, Yale University, New Haven, CT 06511, USA, and Department of Pathology, Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA. J. Hsiao, D. S. Fay, D. F. Stern, Department of Pathology,Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA.
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- David S. Fay
- Z. Sun, Department of Biology, Yale University, New Haven, CT 06511, USA, and Department of Pathology, Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA. J. Hsiao, D. S. Fay, D. F. Stern, Department of Pathology,Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA.
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- David F. Stern
- Z. Sun, Department of Biology, Yale University, New Haven, CT 06511, USA, and Department of Pathology, Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA. J. Hsiao, D. S. Fay, D. F. Stern, Department of Pathology,Yale School of Medicine, 310 Cedar Street, Room BML 342, New Haven, CT 06520–8023, USA.
書誌事項
- 公開日
- 1998-07-10
- DOI
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- 10.1126/science.281.5374.272
- 公開者
- American Association for the Advancement of Science (AAAS)
この論文をさがす
説明
<jats:p> The Rad53 protein kinase of <jats:italic>Saccharomyces cerevisiae</jats:italic> 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 <jats:sub>2</jats:sub> /M cell cycle phase arrest, and increase of <jats:italic>RNR3</jats:italic> 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. </jats:p>
収録刊行物
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- Science
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Science 281 (5374), 272-274, 1998-07-10
American Association for the Advancement of Science (AAAS)