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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Haschemeyer, A. E. V., Proc. natn. Acad. Sci. U.S.A., 62, 128–135 (1969).
Mathews, R. W., Oronsky, A., and Haschemeyer, A. E. V., J. biol. Chem., 248, 1329–1333 (1973).
Scornik, O. A., J. biol. Chem., 249, 3876–3883 (1974).
Mathews, R. W., and Haschemeyer, A. E. V., Biochim. biophys. Acta, 425, 220–228 (1976).
Haschemeyer, A. E. V., Comp. Biochem. Physiol., 28, 535–552 (1969).
Willis, D. B., and Starr, J. L., J. biol. Chem., 246, 2828–2834 (1971).
Slobin, L. I., and Moller, W., Nature, 258, 452–454 (1975).
Hassell, J. A., and Engelhardt, D. L., Biochemistry, 15, 1375–1381 (1976).
Olsnes, A., Spaeren, U., Heiburg, R., and Pihl, A., Biochem. J., 130, 297–299 (1972).
McKeehan, W. L., and Hardesty, B., J. biol. Chem., 244, 4330–4339 (1969).
Siler, J., and Moldave, K., Biochim. biophys. Acta, 195, 123–129 (1969).
Iwasaki, K., Nagata, S., Mizumoto, K., and Kaziro, Y., J. biol. Chem., 249, 5008–5010 (1974).
Moldave, K., Meth. Enzymol., 6, 757–761 (1963).
Nirenberg, M., and Leder, P., Science, 145, 1399–1407 (1964).
Lin, S. Y., McKeehan, W. L., Culp, W., and Hardesty, B., J. biol. Chem., 244, 4340–4350 (1969).
Schaffner, W., and Weissmann, C., Analyt. Biochem., 56, 502–514 (1973).
Nielsen, J. B. K., and Haschemeyer, A. E. V., Biol. Bull., 147, 492–493 (1974).
Haschemeyer, A. E. V., Trends Biochem. Sci. (in the press).
Furano, A. V., Proc. natn. Acad. Sci. U.S.A., 72, 4780–4784 (1975).
McEwen, C. R., Analyt. Biochem., 20, 114–149 (1967).
Nielsen, J. B., and Haschemeyer, A. E. V., Biochemistry, 15, 348–355 (1976).
Schneir, M., and Moldave, K., Biochim. biophys. Acta, 166, 58–57 (1968).
Collins, J. F., Moon, H. M., and Maxwell, E. S., Biochemistry, 11, 4187–4194 (1972).
Lanzani, G. A., et al., Biochim. biophys. Acta, 407, 4780–4784 (1975).
Quintard, B., and Julien, R., FEBS Lett., 57, 285–289 (1975).
Weissbach, H., and Brot, N., Cell, 2, 137–144 (1974).
Iwasaki, K., Mizumoto, K., Tanaka, M., and Kaziro, Y., J. Biochem., 74, 849–852 (1973).
Iwasaki, K., Motoyoshi, K., Nagata, S., and Kaziro, Y., J. biol. Chem., 251 1843–1845 (1976).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/264804a0
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.