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FHA domain boundaries of the Dun1p and Rad53p cell cycle checkpoint kinases
Author(s) -
Hammet Andrew,
Pike Brietta L.,
Mitchelhill Kenneth I.,
Teh Trazel,
Kobe Bostjan,
House Colin M.,
Kemp Bruce E.,
Heierhorst Jörg
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01392-2
Subject(s) - saccharomyces cerevisiae , microbiology and biotechnology , kinase , cell cycle , g2 m dna damage checkpoint , cdc37 , biology , protein kinase domain , protein domain , chek1 , cell cycle checkpoint , function (biology) , gene , genetics , protein kinase a , extracellular signal regulated kinases , mutant
Dun1p and Rad53p of the budding yeast Saccharomyces cerevisiae are members of a conserved family of cell cycle checkpoint protein kinases that contain forkhead‐associated (FHA) domains. Here, we demonstrate that these FHA domains contain 130–140 residues, and are thus considerably larger than previously predicted by sequence comparisons (55–75 residues). In vivo, expression of the proteolytically defined Dun1p FHA domain, but not a fragment containing only the predicted domain boundaries, inhibited the transcriptional induction of repair genes following replication blocks. This indicates that the non‐catalytic FHA domain plays an important role in the transcriptional function of the Dun1p protein kinase.