O. Minella et al., CDC2 KINASE SETS A MEMORY PHOSPHORYLATION SIGNAL ON ELONGATION-FACTOREF-1-DELTA DURING MEIOTIC CELL-DIVISION, WHICH PERDURES IN EARLY DEVELOPMENT, Cellular and molecular biology, 40(4), 1994, pp. 521-525
EF-1 delta is a physiological substrate for cdc2 protein kinase in Xen
opus oocytes The protein is part of the nucleotide exchange factor EF-
1 beta gamma delta, involved in the elongation step of protein synthes
is. We show that EF-1 delta exists under four isoforms in the prophase
oocyte, all phosphorylable by casein kinase II. Each of the prophase
isoforms was further separated into a 36 and a 38 kDa form upon phosph
orylation by cdc2 kinase which therefore reveals the existence of eigh
t different isoforms. Phosphorylation by cdc2 kinase can be monitored
as the electrophoretic mobility dedoublement 36/38 kDa. Developmental
regulation of EF-1 delta was analyzed. The cdc2 kinase-induced change
occures at meiotic division, after complete oogenesis and perdures dur
ing early development. It is therefore a phosphorylation memory signal
for early development.