Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9NSE4 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cybrid cell | transmitochondrial | Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
Isoleucyl-tRNA synthetase | - |
Homo sapiens |
mt isoleucyl-tRNA synthetase | - |
Homo sapiens |
mt-IleRS | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | constitutive high levels of mt isoleucyl-tRNA synthetase (mt-IleRS) are associated with reduced penetrance of the homoplasmic m.4277T>C mt-tRNAIle mutation, causing hypertrophic cardiomyopathy, which is paralleled by results in mutant transmitochondrial cybrids following overexpression of mt-IleRS. Interchangeable ability of three human mt-aaRS, namely mt-ValRS, mt-LeuRS and mt-IleRS, to suppress the mitochondrial functional defects associated with pathogenic homoplasmic mutations in mt-tRNAIle gene (MTTI). Transient overexpression of cognate mt-IleRS causes a 1.5fold increase in the viability of m.4277T>C MTTI mutant cybrids grown in galactose medium. The carboxy-terminal domain of human mt-leucyl-tRNA synthetase is both necessary and sufficient to improve the pathologic phenotype associated either with the mild mutations or with the severe m.3243A>G mutation in the mt-tRNALeu(UUR) gene. This small, non-catalytic domain is able to directly and specifically interact in vitro with human mt-tRNALeu(UUR) with high affinity and stability and, with lower affinity, with mt-tRNAIle | Homo sapiens |
additional information | three human mitochondrial aminoacyl-tRNA syntethases, namely leucyl-, valyl-, and isoleucyl-tRNA synthetase are able to improve both viability and bioenergetic proficiency of human transmitochondrial cybrid cells carrying pathogenic mutations in the mt-tRNAIle gene | Homo sapiens |