Amino acid control of stable RNA synthesis in Friend leukemia cells in relation to intracellular purine nucleoside triphosphate levels.

Histidinol is known to cause deacylation of histidyl-tRNA in cultured mammalian cells, thereby producing a functional deprivation of histidine. Such deprivation of an essential amino acid is known to produce various effects, including inhibition of tRNA synthesis and of nucleolar RNA synthesis and processing. It has been proposed [Grummt, F. & Grummt, I. (1976) Eur. J. Biochem. 64, 307-312] that this response to amino acid deprivation is mediated by decreases in GTP and ATP pool sizes caused by a deacylated-tRNA-dependent hydrolysis of GTP. In contrast, we find that Friend leukemia cells treated with histidinol show no significant changes in GTP or ATP pool sizes, although this treatment does produce the expected inhibition of rRNA and tRNA synthesis.