Abstract
IT is well established that elongation factor 1 (EF1), the enzyme responsible for binding aminoacyl tRNA to ribosomes, exists in multiple forms in a variety of different eukaryotic tissues1–6. It is also generally accepted that in mammalian cells the heavy forms of EF1 (EF1H), with molecular weights ranging from 2×105 to >1×106, represent aggregates of a light form, with a molecular weight of ∼50,000 (refs 4 and 7). The functional significance of these findings remains unclear, since both forms are active in binding aminoacyl tRNA to ribosomes. We report here that the dehydrated gastrulae (cysts) of the brine shrimp, Artemia salina, contain almost exclusively a high molecular weight (∼250,000) form of EF1. During development of the organism EF1H seems to disappear completely so that the free swimming (hatched) embryos (nauplii) contain only a light form of the enzyme (EF1L). This change occurs at or near the time of hatching.
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SLOBIN, L., MÖLLER, W. Changes in form of elongation factor during development of Artemia salina. Nature 258, 452–454 (1975). https://doi.org/10.1038/258452a0
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DOI: https://doi.org/10.1038/258452a0
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