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Literature summary for 6.1.1.5 extracted from

  • Perli, E.; Giordano, C.; Pisano, A.; Montanari, A.; Campese, A.F.; Reyes, A.; Ghezzi, D.; Nasca, A.; Tuppen, H.A.; Orlandi, M.; Di Micco, P.; Poser, E.; Taylor, R.W.; Colotti, G.; Francisci, S.; Morea, V.; Frontali, L.; Zeviani, M.; dAmati, G.
    The isolated carboxy-terminal domain of human mitochondrial leucyl-tRNA synthetase rescues the pathological phenotype of mitochondrial tRNA mutations in human cells (2014), EMBO Mol. Med., 6, 169-182 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Homo sapiens Q9NSE4
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Source Tissue

Source Tissue Comment Organism Textmining
cybrid cell transmitochondrial Homo sapiens
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Synonyms

Synonyms Comment Organism
Isoleucyl-tRNA synthetase
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 Homo sapiens
mt isoleucyl-tRNA synthetase
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 Homo sapiens
mt-IleRS
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 Homo sapiens

General Information

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