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TitleOxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy.
Journal, issue, pagesNucleic Acids Res, Vol. 49, Issue 20, Page 11800-11809, Year 2021
Publish dateNov 18, 2021
AuthorsPooja Srinivas / Rebecca E Steiner / Ian J Pavelich / Ricardo Guerrero-Ferreira / Puneet Juneja / Michael Ibba / Christine M Dunham /
PubMed AbstractHigh fidelity during protein synthesis is accomplished by aminoacyl-tRNA synthetases (aaRSs). These enzymes ligate an amino acid to a cognate tRNA and have proofreading and editing capabilities that ...High fidelity during protein synthesis is accomplished by aminoacyl-tRNA synthetases (aaRSs). These enzymes ligate an amino acid to a cognate tRNA and have proofreading and editing capabilities that ensure high fidelity. Phenylalanyl-tRNA synthetase (PheRS) preferentially ligates a phenylalanine to a tRNAPhe over the chemically similar tyrosine, which differs from phenylalanine by a single hydroxyl group. In bacteria that undergo exposure to oxidative stress such as Salmonella enterica serovar Typhimurium, tyrosine isomer levels increase due to phenylalanine oxidation. Several residues are oxidized in PheRS and contribute to hyperactive editing, including against mischarged Tyr-tRNAPhe, despite these oxidized residues not being directly implicated in PheRS activity. Here, we solve a 3.6 Å cryo-electron microscopy structure of oxidized S. Typhimurium PheRS. We find that oxidation results in widespread structural rearrangements in the β-subunit editing domain and enlargement of its editing domain. Oxidization also enlarges the phenylalanyl-adenylate binding pocket but to a lesser extent. Together, these changes likely explain why oxidation leads to hyperaccurate editing and decreased misincorporation of tyrosine. Taken together, these results help increase our understanding of the survival of S. Typhimurium during human infection.
External linksNucleic Acids Res / PubMed:34581811 / PubMed Central
MethodsEM (single particle)
Resolution3.65 Å
Structure data

24249

7n8y

EMDB-24249, PDB-7n8y:
Oxidized PheRS G318W from Salmonella enterica serovar Typhimurium
Method: EM (single particle) / Resolution: 3.65 Å

Source
  • salmonella enterica subsp. enterica serovar typhimurium (bacteria)
KeywordsRNA BINDING PROTEIN / LIGASE / synthetase / tRNA-binding protein / tetrameric / oxidized

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