AJP - Endocrinology and Metabolism, Vol 264, Issue 2 E257-E263, Copyright © 1993 by American Physiological Society

ARTICLES

Aminoacylation of initiator methionyl-tRNA(i) under conditions inhibitory to initiation of protein synthesis

K. M. Ojamaa, S. R. Kimball and L. S. Jefferson
Department of Cellular and Molecular Physiology, College of Medicine, Pennsylvania State University, Hershey 17033.

Inhibition of protein synthesis in perfused rat liver deprived of either methionine or tryptophan results from a defect in peptide-chain initiation. Similarly, the decreased rate of protein synthesis in liver from rats deprived of food for 24 h and in skeletal muscle after 2 days of diabetes results from a defect in initiation. In the present study, the tissue content of tRNA(iMet) and its level of aminoacylation were measured in these conditions to determine whether methionyl-tRNA(iMet) formation is a mechanism involved in the regulation of initiation. The extent of aminoacylation of tRNA(iMet) in livers perfused with supplemented medium or medium deficient in either methionine or tryptophan was 64 +/- 2, 61 +/- 3, and 66 +/- 2% of the total accepting activity, respectively. The total tissue content of tRNA(iMet), expressed as a percentage of total RNA, was 1.7 +/- 0.1, 1.6 +/- 0.1, and 1.6 +/- 0.1 for the three conditions, respectively. In livers from starved rats, the extent of aminoacylation of tRNA(iMet) was 80 +/- 7% and the total tissue content of tRNA(iMet) was 1.9 +/- 0.1% compared with control values of 82 +/- 6 and 2.0 +/- 0.1%, respectively. In skeletal muscle from diabetic rats, the extent of aminoacylation of tRNA(iMet) was 79 +/- 4% and the total tissue content of tRNA(iMet) was 2.0 +/- 0.3% compared with values of 79 +/- 5 and 2.0 +/- 0.2% for control animals.(ABSTRACT TRUNCATED AT 250 WORDS)

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