Cell Mol Biol (Noisy-le-grand) 1994 Jun 01;404:521-5.

cdc2 kinase sets a memory phosphorylation signal on elongation factor EF-1 delta during meiotic cell division, which perdures in early development.

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EF-1 delta is a physiological substrate for cdc2 protein kinase in Xenopus oocytes. The protein is part of the nucleotide exchange factor EF-1 beta gamma delta, involved in the elongation step of protein synthesis. 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 phosphorylation by cdc2 kinase which therefore reveals the existence of eight 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 during early development. It is therefore a phosphorylation memory signal for early development.

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Species referenced: Xenopus laevis
Genes referenced: cdk1 pold1