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Nucleic Acids Research, 1990, Vol. 18, No. 12 3489-3493
© 1990

MOLECULAR BIOLOGY

Three genes under different developmental control encode elongation factor 1-{alpha} in Xenopus laevis

Marcellin K. Djé, André Mazabraud, Alain Viel, Marc le Maire, Herman Denis, Eric Crawford1,{dagger} and Donald D. Brown1

Centre de Génétique Moléculaire, Laboratoire propre du CNRS associé a I'Université P. et M.Curie (Paris VI) F-91198 Gif-sur-Yvette Cedex, France 1Department of Embryology, Carnegie Institution of Washington 115 W. University Parkway, Baltimore, MD 21210, USA

Revised May 21, 1990. Accepted May 21, 1990.

We have cloned cDNAs encoding two variants of the elongation factor for protein synthesis in Xenopus laevis, called EF-1{alpha}. One of these (42Sp50) is expressed exclusively in immature oocytes. It is one of two protein components of a 42S RNP particle that is very abundant in previtellogenic oocytes. The 42S RNP particle consists of various tRNAs, 5S RNA, 42Sp50 and a 5S RNA binding protein (42Sp43). A major function served by 42Sp50 appears to be the storage of tRNAs for later use in oogenesis and early embryogenesis. The second EF-1{alpha} variant (EF-1{alpha}) is expressed mainly in oocytes but transiently in early embryogenesis as well. Its mRNA cannot be detected after neurulation in somatic cells. EF-1{alpha}O is closely related to a third EF-1{alpha} (EF-1{alpha}S), discovered originally by Krieg et al. (1). EF-1{alpha}S is expressed at low levels in oocytes but actively in somatic cells. The latter two proteins are very similar to known eukaryotic EF-1{alpha} from other organisms and presumably function in their respective cell types to support protein synthesis.

{dagger}Deceased


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