Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Catalytic Domain* / genetics
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Catalytic Domain* / physiology
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Cell Cycle Proteins*
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Checkpoint Kinase 2
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Chymotrypsin / metabolism
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DNA Replication / drug effects
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Gene Expression Regulation, Fungal
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Genes, Fungal / genetics
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Hydroxyurea / pharmacology
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Protein Kinases / chemistry*
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Protein Kinases / genetics
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Protein Kinases / metabolism*
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Protein Serine-Threonine Kinases*
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Protein Structure, Tertiary
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Saccharomyces cerevisiae / drug effects
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins*
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Sequence Alignment
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Serine Endopeptidases / metabolism
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Transcription, Genetic / genetics
Substances
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Cell Cycle Proteins
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Fungal Proteins
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Peptide Fragments
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RNA, Messenger
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Saccharomyces cerevisiae Proteins
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Protein Kinases
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DUN1 protein, S cerevisiae
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Checkpoint Kinase 2
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Protein Serine-Threonine Kinases
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RAD53 protein, S cerevisiae
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Serine Endopeptidases
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Chymotrypsin
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glutamyl endopeptidase
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Hydroxyurea