Abstract
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 (Bellé, 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.
Highlights
Protein synthesis is believed to be under control of the cell cycldeuring meiosis and mitosis
During meiosis of Xenopus laevisoocytes one of the 1P (EF-1P) fromArtemia salina,respectively (8-10). Whether substrates for this kinase is a p47 protein, which is this P47 complex displays activities belonging to elongation complexed to twoother proteins, P36 and P30
Elongation factor l a (EF-la) is responsible for the binding of aminoacyl transfer RNA to theribosome with concomitant hydrolysis of one G T P molecule
Summary
Vol 266, No 23, Issue of August 15, pp. 14885-14888,1991 01991 by The American Society for Biochemistry and Molecular Biology, Inc. During meiosis of Xenopus laevisoocytes one of the 1P (EF-1P) fromArtemia salina,respectively (8-10) Whether substrates for this kinase is a p47 protein, which is this P47 complex displays activities belonging to elongation complexed to twoother proteins, P36 and P30. 1B) oth stimulate elongationfactor l a - The actual guanine nucleotideexchange activity resides in mediated transfer RNA binding to ribosomes and exchange of guanine nucleotides on elongation factor la to a comparable degree. Proteins and Ribosomes-Purification of P47 complex from Xenopus oocytes was performed as described earlier (7). Elongation Factor Assays-The exchange of guanine nucleotides on EF-la and stimulation of Phe-tRNA binding to ribosomes were performed as described in Ref. 15.
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