Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference68 articles.
1. AMINOACYL tRNA SYNTHETASES: GENERAL SCHEME OF STRUCTURE-FUNCTION RELATIONSHIPS IN THE POLYPEPTIDES AND RECOGNITION OF TRANSFER RNAS
2. Specific Sequence Homology and Three-Dimensional Structure of an Aminoacyl Transfer RNA Synthetase
3. Sequence similarities among the family of aminoacyl-tRNA synthetases
4. 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.
5. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
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3. X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications;Nucleic Acids Research;2021-08-14
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