Unraveling the Critical Role Played by Ado762′OH in the Post-Transfer Editing by Archaeal Threonyl-tRNA Synthetase
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada
2. Department of Chemistry, Faculty of Science, Damietta University, New Damietta, Damietta Governorate 34511, Egypt
Funder
Cultural Affairs and Missions Sector, Ministry of Higher Education
Natural Sciences and Engineering Research Council of Canada
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.7b10254
Reference47 articles.
1. Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
2. Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea
3. Aminoacyl-tRNA synthetases: potential markers of genetic code development
4. Double-sieving-defective aminoacyl-tRNA synthetase causes protein mistranslation and affects cellular physiology and development
5. Mechanistic insights into cognate substrate discrimination during proofreading in translation
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