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Literature summary for 6.1.1.4 extracted from

  • Giordano, C.; Morea, V.; Perli, E.; dAmati, G.
    The phenotypic expression of mitochondrial tRNA-mutations can be modulated by either mitochondrial leucyl-tRNA synthetase or the C-terminal domain thereof (2015), Front. Genet., 6, 113 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.4

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-leucine + tRNAIle Homo sapiens
-
 AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q15031
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-leucine + tRNAIle
-
 Homo sapiens AMP + diphosphate + L-leucyl-tRNALeu
-
 ?

Synonyms

Synonyms Comment Organism
leucyl-tRNA syntethase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction mutations in mitochondrial DNA determine important human diseases. The majority of the known pathogenic mutations are located in transfer RNA (tRNA) genes and are responsible for a wide range of currently untreatable disorders. The detrimental effects of mt-tRNA point mutations can be attenuated by increasing the expression of the cognate mt-aminoacyl-tRNA synthetases (aaRSs). The isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) localizes to mitochondria and ameliorates the energetic defect in trans-mitochondrial cybrids carrying mutations either in the cognate mt-tRNALeu(UUR) or in the non-cognate mt-tRNAIle gene.Since the mt-LeuRS-Cterm does not possess catalytic activity, its rescuing ability is most likely mediated by a chaperon-like effect, consisting in the stabilization of the tRNA structure altered by the mutation Homo sapiens
additional information analysis of the bacterial LeuRS structures (PDB IDs 2BTE and 4AS1) reveals that the isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) interacts with the elbow region of the cognate tRNA and establishes a higher number of contacts with the sugar-phosphate backbone than with nucleotide-specific chemical groups, preferred interaction of human mt-LeuRS-Cterm with ribose and phosphate oxygen atoms Homo sapiens