Literature summary for 6.1.1.4 extracted from

Li, R.; Guan, M.X.
Human mitochondrial leucyl-tRNA synthetase corrects mitochondrial dysfunctions due to the tRNALeu(UUR) A3243G mutation, associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like symptoms and diabetes (2010), Mol. Cell. Biol., 30, 2147-2154.

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Application

Application	Comment	Organism
medicine	the A3243G mutation of the tRNALeu gene causes mitochondrial encephalomyopathy, lactic acidosis, and stroke-like symptoms and 2% of cases of type 2 diabetes. The alteration of aminoacylation of tRNALeu(UUR) caused by the A3243G mutation leads to mitochondrial translational defects and thereby reduces the aminoacylating efficiencies of tRNALeu(UUR) as well as of tRNAAla and tRNAMet. The transfer of human mitochondrial leucyl-tRNA synthetase into the cybrid cells carrying the A3243G mutation improve the efficiency of aminoacylation and stability of mitochondrial tRNAs and then increase the rates of mitochondrial translation and respiration, consequently correcting the mitochondrial dysfunction	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Synonyms

Synonyms	Comment	Organism
LARS2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the A3243G mutation of the tRNALeu gene causes mitochondrial encephalomyopathy, lactic acidosis, and stroke-like symptoms and 2% of cases of type 2 diabetes. The alteration of aminoacylation of tRNALeu(UUR) caused by the A3243G mutation leads to mitochondrial translational defects and thereby reduces the aminoacylating efficiencies of tRNALeu(UUR) as well as of tRNAAla and tRNAMet	Homo sapiens

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Release 2023.1 (January 2023)