Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

@article{Eriani1990PartitionOT,
  title={Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs},
  author={Gilbert Eriani and Marc Delarue and Olivier Poch and Jean Gangloff and Dino Moras},
  journal={Nature},
  year={1990},
  volume={347},
  pages={203-206}
}
THE aminoacyl-transfer RNA synthetases (aaRS) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology. Out of the 18 known aaRS, only 9 (ref. 1), referred to as class I synthetases (GlnRS, TyrRS, MetRS, GluRS, ArgRS, ValRS, IleRS, LeuRS, TrpRS), display two short common consensus sequences ('HIGH' and 'KMSKS') which indicate, as observed in… 
Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase
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TLDR
The recognition specificity of a class II aminoacyl-tRNA synthetases (aaRS) and AspRS is reviewed in detail and more stringent sequence homology requirements led to the definition of subclasses.
Two types of aminoacyl-trna synthetases could be originally encoded by complementary strands of the same nucleic ACID
  • S. Rodin, S. Ohno
  • Biology
    Origins of life and evolution of the biosphere
  • 2005
TLDR
It is concluded that these two synthetases emerged synchronously as complementary strands of the same primordial nucleic acid and may explain many intriguing features of aaRSs and favor the elucidation of the origin of the genetic code.
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TLDR
The results underline the existence of an intimate evolutionary link between the aminoacyl-tRNA synthetases, despite their actual structural diversity, and the crucial role of the sequence motifs in substrate binding and enzyme structure is high-lighted.
Region of a conserved sequence motif in a class II tRNA synthetase needed for transfer of an activated amino acid to an RNA substrate.
TLDR
Because D235 in alanine tRNA synthetase is at the beginning of one of the conserved motifs that define class II t RNA synthetases, this region of the structure may in general be important for the transfer step.
Protein-RNA domain-domain interactions in a tRNA sythetase system
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Aminoacyl-tRNA Synthetases in the Bacterial World.
TLDR
Comparisons and differences in the properties of aaRSs from the three kingdoms of life are pinpointed throughout the review and distinctive characteristics of bacterium-like synthetases from organelles are outlined.
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.
TLDR
The crystal structure of a class I aminoacyl-transfer RNA Synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution and showed an all-alpha-helix architecture, an alpha-helIX cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.
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TLDR
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TLDR
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