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J. Biol. Chem., Vol. 266, Issue 23, 14885-14888, Aug, 1991
GM Janssen, J Morales, A Schipper, JC Labbe, O Mulner-Lorillon, R Belle and W Moller
Protein synthesis is believed to be under control of the cell cycle during
meiosis and mitosis. Any relationship between substrates for cdc2 kinase
and components of the protein synthetic apparatus would therefore be of
prime importance. During meiosis of Xenopus laevis oocytes one of the
substrates for this kinase is a p47 protein, which is complexed to two
other proteins, P36 and P30. Judged from partial amino acid sequence data
on P47 and P30, the P30 and P47 proteins were reported to resemble the
protein synthetic elongation factors (EF) 1 beta and 1 gamma from Artemia
salina (Belle, R., Derancourt, J., Poulhe, R., Capony, J.P., Ozon, R., and
Mulner-Lorillon, O. (1989) FEBS Lett. 255, 101-104). This paper shows that
the complex composed of P30, P47, and P36 from Xenopus is identical to the
complex of EF-1 beta, EF- 1 gamma, and EF-1 delta from Artemia according to
two criteria. 1) Both stimulate elongation factor 1 alpha-mediated transfer
RNA binding to ribosomes and exchange of guanine nucleotides on elongation
factor 1 alpha to a comparable degree. 2) Each of the three subunits of the
protein complex P30.P47.P36 from Xenopus shows a structural homology with
one of the corresponding subunits of EF-1 beta gamma delta from Artemia.
Presumably the phosphorylation of EF-1 gamma, which associates with tubulin
at least in vitro, is important in processes following the onset of meiosis
which is accompanied by a rise of protein synthesis.
A major substrate of maturation promoting factor identified as elongation factor 1 beta gamma delta in Xenopus laevis
Department of Medical Biochemistry, Sylvius Laboratory, State University of Leiden, The Netherlands.
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