Abstract
OOCYTES arrested in the G2 phase of the cell cycle contain a p34cdc2/cyclin B complex which is kept in an inactive form by phosphorylation of its p34cdc2 subunit on tyrosine, threonine and perhaps serine residues (see refs 1 and 2 for review). The phos-phatase(s) involved in p34cdc2 dephosphorylation is unknown, but the product of the fission yeast cdc25+ gene3,4, and its homologues in budding yeast5 and Drosophila6 are probably positive regulators of the transition from G2 to M phase. We have purified the inactive p34cdc2/cyclin B complex from G2-arrested starfish oocytes. Addi-tion of the purified bacterially expressed product of the human homologue of the fission yeast cdc25+ gene7 (p54CDC25H) triggers p34cdc2 dephosphorylation and activates HI histone kinase activity in this preparation. We propose that the cdc25+ gene product directly activates the p34cdc2–cyclin B complex.
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Strausfeld, U., Labbé, J., Fesquet, D. et al. Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein. Nature 351, 242–245 (1991). https://doi.org/10.1038/351242a0
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DOI: https://doi.org/10.1038/351242a0
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