Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase.
Sequence comparisons among methionyl-tRNA synthetases from different organisms reveal only one block of homology beyond the last beta strand of the mononucleotide fold. We have introduced a series of semi-conservative amino acid replacements in the conserved motif of yeast methionyl-tRNA synthetase. The results indicate that replacements of two polar residues (Asn584 and Arg588) affected specifically the aminoacylation reaction. The location of these residues in the tertiary structure of the enzyme is compatible with a direct interaction of the amino acid side-chains with the tRNA anticodon.
Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
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Despons
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Walter
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Ebel
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Fasiolo
D000595:Amino Acid Sequence; D000926:Anticodon; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D008718:Methionine-tRNA Ligase / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010957:Plasmids; D011487:Protein Conformation; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D000926:Anticodon; D008718:Methionine-tRNA Ligase