Interaction between dimeric methionyl-tRNA synthetase and methionine accepting tRNAs from E. coli.-- Studies by partial ribonuclease digestion.
Using different ribonucleases we have studied the digestion pattern of the two methionine accepting tRNAs, the initiator tRNAfMet and the elongator tRNAmMet from E. coli. The positions and intensities of cleavages are compared to those obtained when the tRNAs are complexed to methionyl-tRNA synthetase. Our results, in comparison with other studies, suggest a general pattern of interaction between tRNAs and their cognate synthetases including the amino acid stem and the anticodon region. Furthermore a lack of involvement of the central region and especially the extra arm seems to be a unique feature of the initiator tRNAMetf.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D004926:Escherichia coli; D008718:Methionine-tRNA Ligase / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism*
D012346:RNA, Transfer, Amino Acyl; C026464:tRNA(m)(Met), methionine-; D012260:Ribonucleases; D000604:Amino Acyl-tRNA Synthetases; D008718:Methionine-tRNA Ligase