Literature summary for 6.1.1.4 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 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene LARS2, expression analysis, generation of the isolated C-terminal domain of human mt leucyl-tRNA synthetase	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of the isolated C-terminal domain of human mt leucyl-tRNA synthetase, and of DELTACterm mutant	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q15031	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cybrid cell	transmitochondrial, osteosarcoma-derived (143B.TK-) cybrid cell lines from patients	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
LARS2	-	Homo sapiens
Leucyl-tRNA synthetase	-	Homo sapiens
mt leucyl-tRNA synthetase	-	Homo sapiens
mt-LeuRS	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	the C-terminal domain of human mt leucyl-tRNA synthetase is both necessary and sufficient to improve the pathologic phenotype associated either with these mild mutations or with the severe m.3243A>G mutation in the mt-tRNALeu(UUR) gene, overview. The 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. The carboxyterminal domain of human mt leucyl-tRNA synthetase can be used to correct mt dysfunctions caused by mt-tRNA mutations. The Cterm domain of human mt-LeuRS directly interacts with mt-tRNALeu(UUR) and mt-tRNAIle in vitro	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

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Release 2023.1 (January 2023)