| Literature DB >> 9034345 |
F Marini1, A Pellicioli, V Paciotti, G Lucchini, P Plevani, D F Stern, M Foiani.
Abstract
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.Entities:
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Year: 1997 PMID: 9034345 PMCID: PMC1169666 DOI: 10.1093/emboj/16.3.639
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598