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.
Laboratoire de Biologie Cellulaire et Moléculaire, Ecole Normale Supérieure de Lyon, France.
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P
Colas
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C
Launay
A E
AE
van Loon
P
P
Guerrier
D000818:Animals; D016213:Cyclins / Q000378:metabolism*; D004640:Emetine / Q000494:pharmacology; D008677:Metaphase / Q000187:drug effects; D008974:Mollusca; D009865:Oocytes / Q000378:metabolism*; D009866:Oogenesis / Q000187:drug effects
D016213:Cyclins; D004640:Emetine