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. 1974 May;71(5):1857–1861. doi: 10.1073/pnas.71.5.1857

Pleiotropy of hisT Mutants Blocked in Pseudouridine Synthesis in tRNA: Leucine and Isoleucine-V aline Operons

Riccardo Cortese †,*, Raymond Landsberg †, R A Vonder Haar ‡, H E Umbarger ‡, Bruce N Ames †
PMCID: PMC388341  PMID: 4151955

Abstract

The hisT gene codes for an enzyme responsible for the conversion of uridine to pseudouridine (Ψ) in the anticodon region of many tRNA species in Salmonella typhimurium. We have previously shown that a hisT mutant has tRNAHis which lacks pseudouridine in this region and as a consequence has an altered chromatographic behavior. We show here a similar alteration in chromatographic behavior of all tRNALeu and one tRNAIle species from a hisT mutant. By contrast, tRNAVal, which contains no pseudouridine except for the one in the TΨCG sequence, is chromatographically unaltered in a hisT mutant.

The absence of pseudouridine in the anticodon region of tRNA in hisT mutants has been previously shown to cause derepression of the histidine operon. We show here that in hisT mutants the regulation of the leucine and the isoleucine and valine operons is also affected: the enzymes of these operons are refractory to repression by the branched chain amino acids. However, there is no difference between hisT and wild type in the pattern of derepression caused by isoleucine or valine limitation and only a slight difference in the enzyme levels in cells grown on minimal medium.

The alteration in the regulation of branched chain amino acid operons may also explain why hisT mutants are resistant to inhibition of growth by the amino acid analogues 5,5,5-trifluoroleucine, β-hydroxyleucine, and norleucine and by the oligopeptides glycylglycylnorleucine and norleucylnorleucine.

Keywords: amino-acid regulation, Salmonella typhimurium, tRNA chromatography

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Selected References

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