A nuclear factor required for specific translation of cyclin B may control the timing of first meiotic cleavage in starfish oocytes.
In most animals, the rate of cyclin B synthesis increases after nuclear envelope breakdown during the first meiotic cell cycle. We have found that cyclin B-cdc2 kinase activity drops earlier in emetine-treated than in control starfish oocytes, although the protein synthesis inhibitor does not activate the cyclin degradation pathway prematurely. Moreover, protein synthesis is required to prevent meiotic cleavage to occur prematurely, sometimes before chromosomes have segregated on the metaphase plate. In normal conditions, increased synthesis of cyclin B after germinal vesicle breakdown (GVBD) balances cyclin degradation and increases the time required for cyclin B-cdc2 kinase to drop below the level that inhibits cleavage. Taken together, these results point to cyclin B as a possible candidate that could explain the need for increased protein synthesis during meiosis I. Although direct experimental evidence was not provided in the present work, cyclin B synthesis after GVBD may be important for correct segregation of homologous chromosomes at the end of first meiotic metaphase, as shown by a variety of cytological disorders that accompany premature cleavage. Although the overall stimulation of protein synthesis because of cdc2 kinase activation is still observed in oocytes from which the germinal vesicle has been removed before hormonal stimulation, the main increase of cyclin B synthesis normally observed after germinal vesicle breakdown is suppressed. The nuclear factor required for specific translation of cyclin B after GVBD is not cyclin B mRNA, as shown by using a highly sensitive reverse transcription followed by polymerase chain reaction procedure that failed to detect any cyclin B mRNA in isolated germinal vesicles.
Galas
S
S
Centre de Recherches de Biochimie Macromoléculaire, Centre National de la Recherche Scientifique-Institut National de la Santé et de la Recherche Médicale Route de Mende, Montpellier, France.
Barakat
H
H
Dorée
M
M
Picard
A
A
D000705:Anaphase; D000818:Animals; D001483:Base Sequence; D001685:Biological Factors / Q000502:physiology*; D016203:CDC2 Protein Kinase / Q000378:metabolism; D016213:Cyclins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D004527:Egg Proteins / Q000096:biosynthesis* / Q000235:genetics; D004640:Emetine / Q000494:pharmacology; D005786:Gene Expression Regulation; D008540:Meiosis; D008870:Microtubules / Q000187:drug effects / Q000648:ultrastructure; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000378:metabolism; D009865:Oocytes / Q000502:physiology*; D016133:Polymerase Chain Reaction; D014176:Protein Biosynthesis / Q000187:drug effects; D012333:RNA, Messenger / Q000235:genetics; D012194:RNA-Directed DNA Polymerase; D013215:Starfish
D001685:Biological Factors; D016213:Cyclins; D004527:Egg Proteins; D012333:RNA, Messenger; D016203:CDC2 Protein Kinase; D012194:RNA-Directed DNA Polymerase; D004640:Emetine