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Literature summary for 6.1.1.16 extracted from

  • Liu, C.; Gamper, H.; Liu, H.; Cooperman, B.S.; Hou, Y.M.
    Potential for interdependent development of tRNA determinants for aminoacylation and ribosome decoding (2011), Nat. Commun., 2, 329.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information construction of a fusion of a eukaryote-specific domain of human CysRS enabling recognition of the sequence differences in the tertiary core of tRNACys. The fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Synonyms

Synonyms Comment Organism
CysRS
-
 Escherichia coli

General Information

General Information Comment Organism
evolution although the nucleotides in tRNA required for aminoacylation are conserved in evolution, bacterial aminoacyl-transfer RNA synthetases are unable to acylate eukaryote-specific tRNA. Whereas Escherichia coli CysRS cannot acylate human tRNACys, the fusion of a eukaryote-specific domain of human CysRS overcomes the cross-species barrier in human tRNACys. In addition to enabling recognition of the sequence differences in the tertiary core of tRNACys, the fused eukaryotic domain redirects the specificity of Escherichia coli CysRS from the A37 present in bacterial tRNACys to the G37 in mammals. The accuracy of codon recognition on the ribosome is also highly sensitive to the A37G transition in tRNACys Escherichia coli