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

FEBS Lett. 1989 Jul 17;251(1-2):219-24. doi: 10.1016/0014-5793(89)81458-9.

Abstract

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 p34cdc2 (a H1 kinase which is a component of the M-phase promoting factor) and [gamma-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • CDC2 Protein Kinase
  • Casein Kinases
  • Chymotrypsin / metabolism
  • Cyclic AMP / pharmacology
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Growth Substances / metabolism*
  • Maturation-Promoting Factor
  • Meiosis
  • Molecular Weight
  • Oocytes / analysis*
  • Peptide Fragments / metabolism
  • Phosphoproteins / isolation & purification*
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism
  • Serine Endopeptidases / metabolism
  • Xenopus laevis

Substances

  • Growth Substances
  • Peptide Fragments
  • Phosphoproteins
  • Adenosine Triphosphate
  • Cyclic AMP
  • Protein Kinases
  • Casein Kinases
  • CDC2 Protein Kinase
  • Maturation-Promoting Factor
  • Serine Endopeptidases
  • Chymotrypsin
  • glutamyl endopeptidase