Disease relevance of tRNA-Met

• The properties of Escherichia coli tRNAMet f1 and tRNAMet f3 that differ by only one base change, m7G to A at position 47, have been compared structurally by proton magnetic resonance and functionally by the aminoacylation reaction [1].

High impact information on tRNA-Met

• The chromatographic behavior of elongator and initiator tRNAMet on a RPC-5 column indicated that both species are altered structurally in gcd10Delta cells, and analysis of base modifications revealed that 1-methyladenosine (m1A) is undetectable in gcd10Delta tRNA [2].
• Comparison of these genes, of the Nicotiana tRNATyr gene and of a Glycine max tRNAMet gene reveals that plant introns from three different species have no sequence homology and are only 11 to 13 nucleotides long [3].
• These observations are discussed in terms of the presence of a single tRNAMet gene in mammalian mitochondria [4].
• Differences in the processing of dimeric tRNASer-tRNAMet precursors derived from the Schizosaccharomyces pombe sup9 wild-type and opal suppressor genes can be attributed to conformational alterations in the tRNASer anticodon/intron domain [5].
• Changes in tertiary structure accompanying a single base change in transfer RNA. Proton magnetic resonance and aminoacylation studies of Escherichia coli tRNAMet f1 and tRNAMet f3 and their spin-labeled (s4U8) derivatives [1].

Biological context of tRNA-Met

• The absence of summation of the rate of methylation of positionally analogous cytidine residues in tRNA1Val, tRNAPhe, and tRNAMet in the case of simultaneous presence of two substrates in the incubation mixture was demonstrated by the method of mixed substrates [6].

Associations of tRNA-Met with chemical compounds

• The NMR spectra of the two tRNA species in the region between 0 and 4 ppm below 4,4-dimethyl-4-silapentane-1-sulfonic acid (DSS) (methyl and methylene region) were the same except for the absence of the lowest field peak at 3.8 ppm in tRNAMet f3, thus unequivocally identifying this resonance at the methyl group of m7G47 of tRNAMet f1 [1].
• Of the two species of tRNAMet, one can be formylated in the presence of formyl tetrahydrofolate and the transformylase from mycobacteria [7].

Other interactions of tRNA-Met

• It shows higher activity on liver tRNAMet f, tRNAMet m, and tRNALys than on unfractionated liver tRNA [8].

Analytical, diagnostic and therapeutic context of tRNA-Met

• To confirm this notion more clearly, the tertiary structure of Ascaris suum mt tRNAMet was analyzed by NMR using various synthetic tRNAs site-specifically labeled with stable isotopes, which were prepared by a combination of chemical synthesis and enzymatic ligation [9].

References