Evolution of Function of a Fused Metazoan tRNA Synthetase
نویسندگان
چکیده
منابع مشابه
Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.
Phenylalanyl-tRNA synthetases [L-phenylalanine:tRNAPhe ligase (AMP-forming), EC 6.1.1.20] from Escherichia coli, yeast cytoplasm, and mammalian cytoplasm have an unusual conserved alpha 2 beta 2 quaternary structure that is shared by only one other aminoacyl-tRNA synthetase. Both subunits are required for activity. We show here that a single mitochondrial polypeptide from Saccharomyces cerevisi...
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15 صفحه اولTrypanosoma seryl-tRNA synthetase is a metazoan-like enzyme with high affinity for tRNASec.
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aaRSs (aminoacyl-tRNA synthetases) are multi-domain proteins that have evolved by domain acquisition. The anti-codon binding domain was added to the more ancient catalytic domain during aaRS evolution. Unlike in eukaryotes, the anti-codon binding domains of GluRS (glutamyl-tRNA synthetase) and GlnRS (glutaminyl-tRNA synthetase) in bacteria are structurally distinct. This originates from the uni...
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ژورنال
عنوان ژورنال: Molecular Biology and Evolution
سال: 2010
ISSN: 0737-4038,1537-1719
DOI: 10.1093/molbev/msq246