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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
