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Characterization of pathogenic mutations in human mitochondrial alanyl‐tRNA synthetase
Author(s) -
Chihade Joseph,
Kennicott Hannah,
Jessica Makori,
Leon Samuel Diaz,
Donnell Isaac,
Heath Jacob
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.526.32
Subject(s) - aminoacylation , aminoacyl trna synthetase , biology , transfer rna , genetics , mitochondrial disease , phenotype , mitochondrion , mutant , mitochondrial dna , mutation , translation (biology) , microbiology and biotechnology , rna , gene , messenger rna
Translation in mitochondria is dependent on a set of mitochondrial specific aminoacyl‐tRNA synthetases. Defects in these enzymes are related to a range of human diseases. For example, mutations in the human mitochondrial alanyl‐tRNA synthetase (AARS2) have been associated with infantile cardiomyopathy and with adult‐onset leukoencephalopathy. Structural analysis of homology models and haplotype analysis suggests that all pathogenic mutations result to some degree in loss of AARS2 function, and that the severity of the mutation correlates with the observed disease phenotype.(1) We are testing this hypothesis in vitro by examining protein stability, RNA binding, and aminoacylation activity of these mutants. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .