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Molecular and Cellular Biology, September 2003, p. 6300-6314, Vol. 23, No. 17
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.17.6300-6314.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Rad53 Phosphorylation Site Clusters Are Important for Rad53 Regulation and Signaling

Soo-Jung Lee, Marc F. Schwartz,{dagger} Jimmy K. Duong, and David F. Stern*

Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510

Received 13 February 2003/ Returned for modification 7 May 2003/ Accepted 3 June 2003

Budding yeast Rad53 is an essential protein kinase that is phosphorylated and activated in a MEC1- and TEL1-dependent manner in response to DNA damage. We studied the role of Rad53 phosphorylation through mutation of consensus phosphorylation sites for upstream kinases Mec1 and Tel1. Alanine substitution of the Rad53 amino-terminal TQ cluster region reduced viability and impaired checkpoint functions. These substitution mutations spared the basal interaction with Asf1 and the DNA damage-induced interactions with Rad9. However, they caused a decrease in DNA damage-induced Rad53 kinase activity and an impaired interaction with the protein kinase Dun1. The Dun1 FHA (Forkhead-associated) domain recognized the amino-terminal TQ cluster of Rad53 after DNA damage or replication blockade. Thus, the phosphorylation of Rad53 by upstream kinases is important not only for Rad53 activation but also for creation of an interface between Rad53 and Dun1.

* Corresponding author. Mailing address: Department of Pathology, School of Medicine, Yale University, 310 Cedar St., BML 342, New Haven, CT 06510. Phone: (203) 785-4832. Fax: (203) 785-7467. E-mail: df.stern{at}yale.edu.

{dagger} Present address: The Wistar Institute, Philadelphia, PA 19104.

Molecular and Cellular Biology, September 2003, p. 6300-6314, Vol. 23, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.17.6300-6314.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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