PMID: 6426527May 22, 1984Paper

Stimulation of protein synthesis by lysine analogues in lysine-deprived Ehrlich ascites tumour cells

Biochimica Et Biophysica Acta
S A Austin, M J Clemens


This paper describes experiments in which we have investigated the mechanism by which amino acid starvation regulates the initiation of protein synthesis in mammalian cells. We have examined the ability of a range of lysine analogues to stimulate protein synthesis in lysine-deprived mouse Ehrlich ascites tumour cells in culture. Of those analogues tested, only those which are cleaved to lysine intracellularly are capable of restoring protein synthesis to the level seen in fully fed cells. Lysine which is covalently linked to agarose does not stimulate translation. After 5 min incubation of lysine-deprived cells with the analogue lysine p-nitroanilide, the lysine concentration in cell extracts is restored to that found in extracts from fed cells, and protein synthesis is maximally stimulated within 5-10 min. During this period of time there is no increase in the concentration of lysine in the medium. These data indicate that it is the size of the intracellular rather than the extracellular amino acid pool which regulates the rate of protein synthesis during amino acid deprivation.


Feb 1, 1975·Analytical Biochemistry·U Fricke
Apr 15, 1976·European Journal of Biochemistry·F Grummt, I Grummt
Nov 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·L H ThompsonC P Stanners
Dec 16, 1974·European Journal of Biochemistry·W J Van VenrooijL Van Loon-Klaassen
Sep 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·M H VaughanJ Forchhammer
Oct 1, 1973·Molecular Biology Reports·W J van Venrooij, L van Loon-Klaassen

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Dec 31, 1990·Biochemical and Biophysical Research Communications·A R BaydounG E Mann

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