| Literature DB >> 25330800 |
Hugh J McMillan1, Peter Humphreys2, Amanda Smith2, Jeremy Schwartzentruber3, Pranesh Chakraborty2, Dennis E Bulman2, Chandree L Beaulieu2, Jacek Majewski4, Kym M Boycott2, Michael T Geraghty2.
Abstract
Aminoacyl-transfer ribonucleic acid (RNA) synthetases (ARSs) are a group of enzymes required for the first step of protein translation. Each aminoacyl-transfer RNA synthetase links a specific amino acid to its corresponding transfer RNA component within the cytoplasm, mitochondria, or both. Mutations in ARSs have been linked to a growing number of diseases. Lysyl-transfer RNA synthetase (KARS) links the amino acid lysine to its cognate transfer RNA. We report 2 siblings with severe infantile visual loss, progressive microcephaly, developmental delay, seizures, and abnormal subcortical white matter. Exome sequencing identified mutations within the KARS gene (NM_005548.2):c.1312C>T; p.Arg438Trp and c.1573G>A; p.Glu525Lys occurring within a highly conserved region of the catalytic domain. Our patients' phenotype is remarkably similar to a phenotype recently reported in glutaminyl-transfer RNA synthetase (QARS), another bifunctional ARS gene. This finding expands the phenotypic spectrum associated with mutations in KARS and draws attention to aminoacyl-transfer RNA synthetase as a group of enzymes that are increasingly being implicated in human disease.Entities:
Keywords: aminoacyl–tRNA; epilepsy; lysyl-tRNA synthetase; microcephaly; vision disorders
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Year: 2014 PMID: 25330800 DOI: 10.1177/0883073814553272
Source DB: PubMed Journal: J Child Neurol ISSN: 0883-0738 Impact factor: 1.987