Human tRNA synthetase catalytic nulls with diverse functions
| Autor: | Kyle P. Chiang, Wing Hung Wong, Feng Wang, Zhiwen Xu, Paul Schimmel, Kin Fai Au, Wing-Sze Lo, Mingjie Zhang, Min Guo, Elisabeth Gardiner, Ching-Fun Lau, Leslie A. Nangle, Xiang-Lei Yang, Jie J. Zhou, John D. Mendlein |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Multidisciplinary Aminoacyl tRNA synthetase Alternative splicing Computational biology Biology Isozyme Catalysis Recombinant Proteins Amino Acyl-tRNA Synthetases Isoenzymes Alternative Splicing chemistry.chemical_compound Enzyme Biochemistry chemistry Organ Specificity Catalytic Domain RNA splicing Transfer RNA Humans Protein Isoforms Gene |
| Zdroj: | Science. 345:328-332 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | Evolving from an enzyme and into a regulator Proteins, the work-horses of the cell, are made on a messenger RNA (mRNA) template. An enzyme called aminoacyl tRNA synthetases (AARSs) attaches the correct amino acid to a transfer RNA so that mRNA is accurately translated. Over evolution, additional sequences have been added to AARSs. Lo et al. found a large number of AARS variants in which the domain responsible for enzyme function was deleted. Ninety-four such variants had diverse signaling activities. Thus, AARSs are used both as enzymes and alternately as regulators of signaling pathways. Science , this issue p. 328 |
| Databáze: | OpenAIRE |
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