Abstract
GENETIC studies in the fission yeast Schizosaccharomyces pombe have established that a critical element required for the G2-→ M-phase transition in the cell cycle is encoded by the cdc2+ gene1–5. The product of this gene is a serine/threonine protein kinase, designated p34cdc2, that is highly conserved functionally from yeast to man2 and has a relative molecular mass of 34,000 (34 K). Purified maturation-promoting factor (MPF) is a complex of p34cdc2 and a 45K substrate that appears in late G2 phase and is sufficient to drive cells into mitosis6–9. This factor has been identified in all eukaryotic cells10,11, and in vitro histone H1 is the preferred substrate for phosphorylation7,9,12. The increase in the activity of HI kinase in M-phase is associated with a large increase in total cell protein phosphorylation which is believed to be a consequence of MPF activation13–18. We show here that the HI kinase activity of p34cdc2 oscillates during the cell cycle in Xenopus, and maximal activity correlates with the dephosphorylated state of p34cdc2. Direct inactivation of MPF in vitro is accompanied by phosphorylation of p34cdc2 and reduction of its protein kinase activity.
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Gautier, J., Matsukawa, T., Nurse, P. et al. Dephosphorylation and activation of Xenopusp34cdc2 protein kinase during the cell cycle. Nature 339, 626–629 (1989). https://doi.org/10.1038/339626a0
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DOI: https://doi.org/10.1038/339626a0
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