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• W1972325857 abstract "The B subunit of the DNA polymerase (pol) α-primase complex executes an essential role at the initial stage of DNA replication in Saccharomyces cerevisiae and is phosphorylated in a cell cycle-dependent manner. In this report, we show that the four subunits of the yeast DNA polymerase α-primase complex are assembled throughout the cell cycle, and physical association between newly synthesized pol α (p180) and unphosphorylated B subunit (p86) occurs very rapidly. Therefore, B subunit phosphorylation does not appear to modulate p180•p86 interaction. Conversely, by depletion experiments and by using a yeast mutant strain, which produces a low and constitutive level of the p180 polypeptide, we found that formation of the p180•p86 subcomplex is required for B subunit phosphorylation. The B subunit of the DNA polymerase (pol) α-primase complex executes an essential role at the initial stage of DNA replication in Saccharomyces cerevisiae and is phosphorylated in a cell cycle-dependent manner. In this report, we show that the four subunits of the yeast DNA polymerase α-primase complex are assembled throughout the cell cycle, and physical association between newly synthesized pol α (p180) and unphosphorylated B subunit (p86) occurs very rapidly. Therefore, B subunit phosphorylation does not appear to modulate p180•p86 interaction. Conversely, by depletion experiments and by using a yeast mutant strain, which produces a low and constitutive level of the p180 polypeptide, we found that formation of the p180•p86 subcomplex is required for B subunit phosphorylation." @default.
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• W1972325857 date "1996-04-01" @default.
• W1972325857 modified "2023-10-17" @default.
• W1972325857 title "Phosphorylation of the DNA Polymerase -Primase B Subunit Is Dependent on Its Association with the p180 Polypeptide" @default.
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• W1972325857 doi "https://doi.org/10.1074/jbc.271.15.8661" @default.
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