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Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34 cdc2 substrate
Author(s) -
Mulner-Lorillon Odile,
Poulhe Robert,
Cormier Patrick,
Labbe Jean-Claude,
Doree Marcel,
Belle Robert
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81458-9
Subject(s) - xenopus , phosphoprotein , maturation promoting factor , in vivo , phosphorylation , cyclin dependent kinase 1 , biology , in vitro , protein kinase a , molecular mass , kinase , microbiology and biotechnology , biochemistry , cell cycle , cell , enzyme , genetics , gene
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‐ 32 P]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.