AbstractComparison of the amino-acid sequences of several methionyl-tRNA synthetases indicates the occurrence of a few conserved motifs, having a possible functional significance. The role of one of these motifs, centered at position 300 in theE. coli enzyme sequence, was assayed by the use of site-directed mutagenesis. Substitution of the His301 or Trp305 residues by Ala resulted in a large decrease in methionine affinity, whereas the change of Val298 into Ala had only a moderate effect. The catalytic rate of the enzyme was unimpaired by these substitutions. It is concluded that the above conserved amino-acid region is located at or close to the amino-acid binding pocket of methionyl-tRNA synthetase
Recent computation analyses have pointed out an existence of conserved amino add motifs among RNA ri...
ABSTRACT: A highly conserved threonine residue marks the amino acid binding pocket within the editin...
International audienceValyl-tRNA synthetase (ValRS) from Escherichia coli undergoes covalent valylat...
AbstractComparison of the amino-acid sequences of several methionyl-tRNA synthetases indicates the o...
International audienceAlignment of the sequences of methionyl-tRNA synthetases from various microbia...
AbstractSequence comparisons among methionyl-tRNA synthetases from different organisms reveal only o...
International audienceBinding of methionine to methionyl-tRNA synthetase (MetRS) is known to promote...
International audiencePolypeptides containing β-amino acids are attractive tools for the design of n...
International audienceMethionyl-adenylate, the mixed carboxylic-phosphoric acid anhydride synthesize...
The accuracy of in vivo incorporation of amino acids during protein biosynthesis is controlled to a ...
International audienceMethionyl-tRNA synthetase (MetRS) from Bacillus stearothermophilus was shown t...
Recent computation analyses have pointed out an existence of conserved amino add motifs among RNA ri...
ABSTRACT: A highly conserved threonine residue marks the amino acid binding pocket within the editin...
International audienceValyl-tRNA synthetase (ValRS) from Escherichia coli undergoes covalent valylat...
AbstractComparison of the amino-acid sequences of several methionyl-tRNA synthetases indicates the o...
International audienceAlignment of the sequences of methionyl-tRNA synthetases from various microbia...
AbstractSequence comparisons among methionyl-tRNA synthetases from different organisms reveal only o...
International audienceBinding of methionine to methionyl-tRNA synthetase (MetRS) is known to promote...
International audiencePolypeptides containing β-amino acids are attractive tools for the design of n...
International audienceMethionyl-adenylate, the mixed carboxylic-phosphoric acid anhydride synthesize...
The accuracy of in vivo incorporation of amino acids during protein biosynthesis is controlled to a ...
International audienceMethionyl-tRNA synthetase (MetRS) from Bacillus stearothermophilus was shown t...
Recent computation analyses have pointed out an existence of conserved amino add motifs among RNA ri...
ABSTRACT: A highly conserved threonine residue marks the amino acid binding pocket within the editin...
International audienceValyl-tRNA synthetase (ValRS) from Escherichia coli undergoes covalent valylat...