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The rat oocyte provides an interesting system in which to dissect the control mechanisms involved in the transition between a meiotic M phase and a mitotic interphase. In this study, we show that in rat oocytes activated parthenogenetically by puromycin, okadaic acid (a potent inhibitor of protein phosphatases 1 and 2A) induced an increase in histone H1 kinase activity suggesting that MPF was reactivated. However, the inhibition of phosphatases 1 and 2A shortly after second polar body extrusion did not allow the formation of a metaphase-like spindle, although microtubule polymerization was not inhibited. Instead, the chromatin remained condensed as a single mass and a large aster formed around it.

Full activation of the rat oocyte by protein synthesis inhibition requires protein phosphatase activity.