Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 23, Issue 17, Pages 6300-6314Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.23.17.6300-6314.2003
Keywords
-
Categories
Funding
- NCI NIH HHS [R01 CA082257, R01CA82257] Funding Source: Medline
- NIGMS NIH HHS [T32 GM007223, T32GM07223] Funding Source: Medline
Ask authors/readers for more resources
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 Tell. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available