1-METHYLGUANOSINE DEFICIENCY OF TRANSFER-RNA INFLUENCES COGNATE CODONINTERACTION AND METABOLISM IN SALMONELLA-TYPHIMURIUM

1-Methylguanosine (m(1)G) is present next to the 3' end of the anticod on (position 37) tRNA(1,2,3)(Leu),tRNA(1,2,3)(Pro), and tRNA(3)(Arg). A mutant of Salmonella typhimurium lacks m(1)G in these seven tRNAs wh en grown at or above 37 degrees C, as a result of a mutation (trmD3) i n the structural gene (trmD) for the tRNA(m(1)G37) methyltransferase. The m(1)G deficiency induced 24 and 26% reductions in the growth rate and polypeptide chain elongation rate, respectively, in morpholineprop anesulfonic acid (MOPS)-glucose minimal medium at 37 degrees C. The ex pression of the leuABCD operon is controlled by the rate with which tR NA(2)(Leu) and tRNA(3)(Leu) read four leucine codons in the leu-leader mRNA, Lack of m(1)G in these tRNAs did not influence the expression o f this operon, suggesting that m(1)G did not influence the efficiency of tRNA(2,3)(Leu). Since the average step time of the m(1)G-deficient tRNAs was 2,3' increased 3.3-fold, the results suggest that the impact of m(1)G in decoding cognate codons may be tRNA dependent, The trmD3 mutation rendered the cell more resistant or sensitive to several amin o acid analogs, 3-Nitro-L-tyrosine (NT), to which the trmD3 mutant is sensitive, was shown to be transported by the tryptophan-specific perm ease, and mutations in this gene mtr) render the cell resistant to NT. Since the trmD3 mutation did not affect the activity of the permease, some internal metabolic step(s), but not the uptake of the analog per se, is affected, We suggest that the trmD3-mediated NT sensitivity is by an abnormal translation of some mRNA(s) whose product(s) is involv ed in the metabolic reactions affected by the analog, Our results also suggest that tRNA modification may be a regulatory device for gene ex pression.