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Histidyl tRNA Synthetase (HARS) is a member of the aminoacyl tRNA synthetase (ARS) family of enzymes. This family of 20 enzymes is responsible for attaching specific amino acids to their cognate tRNA molecules, a critical step in protein synthesis. However, recent work highlighting a growing number of associations between ARS genes and diverse human diseases raises the possibility of new and unexpected functions in this ancient enzyme family. For example, mutations in HARS have been linked to two different neurological disorders, Usher Syndrome Type IIIB and Charcot Marie Tooth peripheral neuropathy. These connections raise the possibility of previously undiscovered roles for HARS in metazoan development, with alterations in these functions leading to complex diseases. In an attempt to establish  Danio rerio  as a model for studying HARS functions in human disease, we characterized the  Danio rerio hars  gene and compared it to that of human  HARS . Using a combination of bioinformatics, molecular biology, and cellular approaches, we found that while the human genome encodes separate genes for cytoplasmic and mitochondrial HARS protein, the  Danio rerio  genome encodes a single  hars  gene which undergoes alternative splicing to produce the respective cytoplasmic and mitochondrial versions of Hars. Nevertheless, while the  HARS  genes of humans and  Danio  differ significantly at the genomic level, we found that they are still highly conserved at the amino acid level, underscoring the potential utility of  Danio rerio  as a model organism for investigating HARS function and its link to human diseases  in vivo .

A single Danio rerio hars gene encodes both cytoplasmic and mitochondrial histidyl-tRNA synthetases