FEBS Letters
Volume 518, Issue 1 , Pages 23-28, 8 May 2002

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

Edited by Julio Celis

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

Received 5 March 2002; accepted 20 March 2002.

Abstract 

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.

Keywords:  cAMP-dependent protein kinase, Chromosome condensation, Histone H3 phosphorylation, Mitogen-activated protein kinase, Oocyte maturation

Abbreviations:  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

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(02)02630-3

FEBS Letters
Volume 518, Issue 1 , Pages 23-28, 8 May 2002