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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‐1γ and EF‐1β
Author(s) -
Bellé Robert,
Derancourt Jean,
Poulhe Robert,
Capony Jean-Paul,
Ozon René,
Mulner-Lorillon Odile
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)81069-5
Subject(s) - xenopus , elongation factor , eukaryotic translation elongation factor 1 alpha 1 , casein kinase 2 , protein kinase a , in vivo , elongation , biology , phosphorylation , maturation promoting factor , substrate (aquarium) , microbiology and biotechnology , homologous chromosome , chemistry , biochemistry , cell , cell cycle , cyclin dependent kinase 2 , gene , genetics , cyclin , ribosome , rna , materials science , ultimate tensile strength , metallurgy , ecology
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 p34 cdc2 . From polypeptide sequencing, we now show that the p30 and the p47 correspond to elongation factor EF‐1β and EF‐1γ. Furthermore, the p30 and p36 proteins were phosphorylated in vitro by casein kinase II.