A role for DNA primase in coupling DNA replication to DNA damage response.
The temperature-sensitive yeast DNA primase mutant pri1-M4 fails to execute an early step of DNA replication and exhibits a dominant, allele-specific sensitivity to DNA-damaging agents. pri1-M4 is defective in slowing down the rate of S phase progression and partially delaying the G1-S transition in response to DNA damage. Conversely, the ... G2 DNA damage response and the S-M checkpoint coupling completion of DNA replication to mitosis are unaffected. The signal transduction pathway leading to Rad53p phosphorylation induced by DNA damage is proficient in pri1-M4, and cell cycle delay caused by Rad53p overexpression is counteracted by the pri1-M4 mutation. Altogether, our results suggest that DNA primase plays an essential role in a subset of the Rad53p-dependent checkpoint pathways controlling cell cycle progression in response to DNA damage.
Mesh Terms:
Blotting, Western, Cell Cycle, Cell Cycle Proteins, DNA, DNA Damage, DNA Primase, DNA Replication, Enzyme Stability, Flow Cytometry, Fungal Proteins, Gene Expression Regulation, Fungal, Genes, Fungal, Interphase, Methyl Methanesulfonate, Mitosis, Models, Biological, Mutagenesis, Site-Directed, Mutagens, Mutation, Phosphorylation, Protein Kinases, Protein-Serine-Threonine Kinases, RNA Nucleotidyltransferases, S Phase, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Temperature, Ultraviolet Rays
Blotting, Western, Cell Cycle, Cell Cycle Proteins, DNA, DNA Damage, DNA Primase, DNA Replication, Enzyme Stability, Flow Cytometry, Fungal Proteins, Gene Expression Regulation, Fungal, Genes, Fungal, Interphase, Methyl Methanesulfonate, Mitosis, Models, Biological, Mutagenesis, Site-Directed, Mutagens, Mutation, Phosphorylation, Protein Kinases, Protein-Serine-Threonine Kinases, RNA Nucleotidyltransferases, S Phase, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Temperature, Ultraviolet Rays
EMBO J.
Date: Feb. 03, 1997
PubMed ID: 9034345
View in: Pubmed Google Scholar
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