A Multifunctional Repeated Motif Is Present in Human Bifunctional tRNA Synthetase
| Autor: | Jong Sang Lee, Sunghoon Kim, Key Sun Kim, Seung Bae Rho, Eui Jun Jeong, Yang Gyun Kim |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Isoleucine-tRNA Ligase
Magnetic Resonance Spectroscopy Protein Conformation Molecular Sequence Data Cell Biology Biochemistry Amino Acyl-tRNA Synthetases chemistry.chemical_compound Tandem repeat Nucleic Acids medicine Animals Humans Amino Acid Sequence Bifunctional Molecular Biology Helix-Turn-Helix Motifs chemistry.chemical_classification Calorimetry Differential Scanning Biomolecule Cell Biology EPRS Dissociation constant Glutamate-tRNA Ligase Drosophila melanogaster medicine.anatomical_structure chemistry Transfer RNA Nucleic acid Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 273:11267-11273 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.273.18.11267 |
| Popis: | Tandem repeats located in the human bifunctional glutamyl-prolyl-tRNA synthetase (EPRS) have been found in many different eukaryotic tRNA synthetases and were previously shown to interact with another distinct repeated motifs in human isoleucyl-tRNA synthetase. Nuclear magnetic resonance and differential scanning calorimetry analyses of an isolated EPRS repeat showed that it consists of a helix-turn-helix with a melting temperature of 59 degrees C. Specific interaction of the EPRS repeats with those of isoleucyl-tRNA synthetase was confirmed by in vitro binding assays and shown to have a dissociation constant of approximately 2.9 microM. The EPRS repeats also showed the binding activity to the N-terminal motif of arginyl-tRNA synthetase as well as to various nucleic acids, including tRNA. Results of the present work suggest that the region comprising the repeated motifs of EPRS provides potential sites for interactions with various biological molecules and thus plays diverse roles in the cell. |
| Databáze: | OpenAIRE |
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