Histone H3 phosphorylation during Xenopus oocyte maturation: regulation by the MAP kinase/p90Rsk pathway and uncoupling from DNA condensation

FEBS Letters

Schmitt, Anja¹  Nebreda, Angel R¹  Lénárt, Péter¹  Ellenberg, Jan¹  Gutierrez, Gustavo J¹ 

[1]European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany

关键词: cAMP-dependent protein kinase;    Chromosome condensation;    Histone H3 phosphorylation;    Mitogen-activated protein kinase;    Oocyte maturation;    CHX;    cycloheximide;    GVBD;    germinal vesicle breakdown;    H1K;    histone H1 kinase;    MAPK;    mitogen-activated protein kinase;    MPF;    maturation promoting factor;    PKA;    cAMP-dependent protein kinase;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(02)02630-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Here we show that during the meiotic maturation of Xenopus oocytes, histone H3 becomes phosphorylated on serine-10 at about the time of maturation promoting factor activation and meiosis I entry. However, overexpression of cAMP-dependent protein kinase that blocks entry into M phase, also leads to massive serine-10 phosphorylation of histone H3 in intact Xenopus oocytes but does not cause chromosome condensation. We also show that the phosphorylation of histone H3 during oocyte maturation requires the activation of the mitogen-activated protein kinase/p90Rsk pathway. Our results indicate that in G2-arrested oocytes, which are about to enter M phase, histone H3 phosphorylation is not sufficient for chromosome condensation.

【 授权许可】

Unknown