Abstract
THE development of rapid kinetic methods for measurement of elongation rate in protein synthesis in vivo, independent of initiation rate, has made possible the study of the control of elongation in relation to changes in overall protein synthesis1–4. In rat liver a 40% reduction in elongation rate (from about six to four amino acid residues per ribosome) is associated with thyroparathyroidectomy2,4; the normal rate is restored by triiodothyronine injections2. The work reported here concerns the role of polypeptide elongation factor 1 (EF1), the factor responsible for aminoacyl-tRNA binding to ribosomes, in the control of elongation rate in this system. Several studies have suggested that EF1 may have regulatory significance in eukaryotic systems5,8; however no direct correlation between EF1 activity and elongation rate in vivo has previously been described.
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NIELSEN, J., PLANT, P. & HASCHEMEYER, A. Polypeptide elongation factor 1 and the control of elongation rate in rat liver in vivo. Nature 264, 804–806 (1976). https://doi.org/10.1038/264804a0
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DOI: https://doi.org/10.1038/264804a0
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