Reference: Ferrari M, et al. (1996) Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide. J Biol Chem 271(15):8661-6

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Abstract


The B subunit of the DNA polymerase (pol) alpha-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 alpha-primase complex are assembled throughout the cell cycle, and physical association between newly synthesized pol alpha (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.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Ferrari M, Lucchini G, Plevani P, Foiani M
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