Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34cdc2 substrate

FEBS Letters

Labbe, Jean-Claude¹  Doree, Marcel¹  Mulner-Lorillon, Odile²  Poulhe, Robert²  Cormier, Patrick²  Belle, Robert² 

[1] Centre de Recherches de Biochimie Macromoléculaire, INSERM U249, UPR CNRS 41, Route de Mende, BP 5051, 34033 Montpellier, France;Laboratoire dephysiologie de la Reproduction, INRA, UA CNRS 555, Université Pierre et Marie Curie, 4 Place Jussieu, 75252 Paris Cedex 05 France

关键词: Protamine kinase;    Meiosis;    Promoting factor;    M-phase;   

DOI  :  10.1016/0014-5793(89)81458-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This paper describes the purification of a 47 kDa protein from Xenopus laevis oocytes that becomes phosphorylated when the oocytes undergo meiotic maturation. This protein (p47) is part of a high molecular mass complex containing at least two other proteins of molecular mass 30 and 36 kDa. This complex can be isolated from stage VI oocytes before maturation. We obtained a pattern for phosphopeptides in p47 phosphorylated in vivo very similar to that of the purified protein phosphorylated in vitro by p34^cdc2 (a H1 kinase which is a component of the M-phase promoting factor) and [γ-³²P]ATP. Therefore, the purified p47, already described as a marker of MPF activity, is the first reported in vivo substrate for the cell division control kinase.

【 授权许可】

Unknown