FHA domain boundaries of the Dun1p and Rad53p cell cycle checkpoint kinases


Autoria(s): Hammet, A; Pike, BL; Mitchelhill, KI; Teh, T; Kobe, B; House, CM; Kemp, BE; Heierhorst, J
Data(s)

01/01/2000

Resumo

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 FI-IA domain plays an important role in the transcriptional function of the Dun1p protein kinase. (C) 2000 Federation of European Biochemical Societies.

Identificador

http://espace.library.uq.edu.au/view/UQ:36353

Idioma(s)

eng

Palavras-Chave #Biochemistry & Molecular Biology #Biophysics #Cell Biology #Forkhead-associated Domain #Dun1p #Rad53p #Chk2 #Protein Kinase #Cell Cycle #Protein-kinase #Dna-damage #Yeast #Replication #Transcription #Phosphatase #Expression #Pathways #Cds1 #Atm
Tipo

Journal Article