A purified complex from Xenopus oocytes contains a p47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF-1 gamma and EF-1 beta.
A high molecular mass complex isolated from Xenopus laevis oocytes contains three main proteins, respectively p30, p36 and p47. The p47 protein has been reported to be an in vivo substrate of the cell division control protein kinase p34cdc2. From polypeptide sequencing, we now show that the p30 and the p47 correspond to elongation factor EF-1 beta and EF-1 gamma. Furthermore, the p30 and p36 proteins were phosphorylated in vitro by casein kinase II.
Bellé
R
R
Laboratoire de Physiologie de la Reproduction, INRA, UA CNRS 555, Paris, France.
Derancourt
J
J
Poulhe
R
R
Capony
J P
JP
Ozon
R
R
Mulner-Lorillon
O
O
D000595:Amino Acid Sequence; D000818:Animals; D047388:Casein Kinases; D004591:Electrophoresis, Polyacrylamide Gel; D006133:Growth Substances / Q000378:metabolism*; D016200:Maturation-Promoting Factor; D008969:Molecular Sequence Data; D009865:Oocytes / Q000032:analysis*; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000302:isolation & purification*; D010455:Peptides / Q000302:isolation & purification; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011506:Proteins / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid; D014981:Xenopus
D006133:Growth Substances; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D010455:Peptides; D011506:Proteins; D011494:Protein Kinases; D047388:Casein Kinases; D016200:Maturation-Promoting Factor