Aminoacyl-tRNA synthetases are multivalent suppressors of defects due to human equivalent mutations in yeast mt tRNA genes
| Autor: | Silvia Francisci, Arianna Montanari, Laura Frontali, Cristina De Luca |
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| Rok vydání: | 2010 |
| Předmět: |
Cell Respiration
Molecular Sequence Data Mutant Mitochondrial diseases Saccharomyces cerevisiae Mitochondrion Biology Amino Acyl-tRNA Synthetases chemistry.chemical_compound RNA Transfer Yeasts mitochondria mitochondrial diseases aminoacyl-trna synthetase Humans Genes Tumor Suppressor Molecular Biology Gene chemistry.chemical_classification Base Sequence Organisms Genetically Modified Aminoacyl tRNA synthetase Cell Biology Yeast Mitochondria Elongation factor Genes Mitochondrial Phenotype Enzyme Amino Acid Substitution Biochemistry chemistry Mutation Transfer RNA Aminoacyl-tRNA synthetase |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1803:1050-1057 |
| ISSN: | 0167-4889 |
| Popis: | The use of the yeast model for the study of the molecular and cellular effects of the pathogenic base substitutions in human mitochondrial tRNA genes has recently been validated by the finding that the suppressing factors identified in yeast (the mitochondrial protein elongation factor EF-Tu and the cognate aminoacyl-tRNA synthetase) have suppressing activities also in human cells. In this paper we report a detailed analysis of the cross-suppressing activities of valyl- and leucyl-tRNA synthetases on different tRNA mutants. Glycerol growth, respiration, Northern analysis consistently show that similar suppressing effects can be obtained by these two yeast synthetases and by the orthologous human enzymes. As a whole the present data indicate that the suppression by mt aa-RS is probably not related to the enzyme activities per se, and may be due to a stabilizing chaperon-like effect of the synthetase molecules on the tRNA structure altered by the mutations. |
| Databáze: | OpenAIRE |
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