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Search for Difference in Aminoacylation of Mitochondrial DNA‐encoded Wild‐type and Mutant Human tRNALeu?(UUR)
Author(s) -
ZhenCheng Wang,
XueMin Wang,
YouXin Jin,
BingHua Jiao,
Feng Xu,
MingYong Miao,
KeJun Zhu
Publication year - 2003
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/1521654031000110190
Subject(s) - aminoacylation , biology , mutant , mitochondrial dna , genetics , transfer rna , point mutation , mutation , mitochondrion , microbiology and biotechnology , gene , rna
The pathogenetic mechanism of the most extensively investigated A3243G mutated tRNALeu (UUR) gene, which causes the MELAS encephalomyopathy, maternally inherited diabetes, or chronic progressive external ophlthalmoplegia, is still unresolved, despite the numerous investigations on the topic. Previous evidences presented in published work suggested that the mitochondrial DNA harboring A3243G mutation result decreases in the rates of mitochondrial protein synthesis. To search for differences in aminoacylation of mitochondrial DNA‐encoded wild‐type and mutant human tRNALeu (UUR), we have expressed and purified the two kinds of tRNAsLeu (UUR), and have expressed human mitochondrial leucyl‐tRNA synthetase for in vitro assays of aminoacylation of wild‐type and mutant human tRNALeu (UUR). The results indicate human mitochondrial tRNALeu (UUR) gene A3243G point mutant can remarkably reduce its aminoacylation, suggesting it could be one of the mechanisms that the mutation can produce in such clinical phenotypes. IUBMB Life, 55: 139‐144, 2003