Protein synthesis controls cyclin stability in metaphase I-arrested oocytes of Patella vulgata.

The metaphasic block of Patella vulgata oocytes depends on protein synthesis as an emetine treatment triggers metaphase/anaphase transition and leads to the sequential disappearance of cyclin A and B. Both cyclins are stable in metaphase-arrested oocytes which indicates that inhibition of protein synthesis activates cyclin proteolysis. The use of extracts prepared from metaphase-arrested oocytes and from emetine-treated oocytes fully confirms these in vivo findings. Considering previous observations about the regulation of protein synthesis throughout the cell cycle, we propose the involvement of a transient inhibition of translation in the activation of cyclin proteolysis and in exit from the M-phase arrest.