A domain for editing by an archaebacterial tRNA synthetase
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference50 articles.
1. Specific Sequence Homology and Three-Dimensional Structure of an Aminoacyl Transfer RNA Synthetase
2. Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases.
3. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
4. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
5. Escherichia coli threonyl-tRNA synthetase and tRNAThr modulate the binding of the ribosome to the translational initiation site of the ThrS mRNA
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1. The role of tRNA identity elements in aminoacyl-tRNA editing;Frontiers in Microbiology;2024-07-18
2. A standalone editing protein deacylates mischarged canavanyl-tRNAArg to prevent canavanine incorporation into proteins;Nucleic Acids Research;2023-01-11
3. A review on quality control agents of protein translation – The role of Trans-editing proteins;International Journal of Biological Macromolecules;2022-02
4. Amino Acid Specificity of Ancestral Aminoacyl-tRNA Synthetase Prior to the Last Universal Common Ancestor Commonote commonote;Journal of Molecular Evolution;2022-01-27
5. Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy;Nucleic Acids Research;2021-09-28
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