Serine–tRNA ligase, cytoplasmic, also called seryl-tRNA synthetase 1 is an enzyme that in humans is encoded by the gene SARS1 (previously SARS). SARS belongs to the class II amino-acyl tRNA family and is found in all humans, and functions as a serine–tRNA ligase which is involved in protein translation and is related to several bacterial and yeast counterparts.
Discovery
Since the 1960s, seryl-tRNA synthetases have been described in various eukaryotic species, in both biochemical and structural analyses. It was not until 1997 that human SARS and its enzyme product were isolated and expressed in Escherichia coli by a team from The European Molecular Biology Laboratory in France.
Gene location
The human SARS gene is located on the plus strand of chromosome 1, from base pair 109,213,893 to base pair 109,238,182.UniProt:
Protein
Seryl-tRNA synthetase is made up of 514 amino acid residues as weighs 58,777 Da."UnitProt" It exists as a homodimer of two identical subunits, with the tRNA molecule binding across the dimer by similarity. It has two distinct domains:
A catalytic core A 3 base pair serine binding N-terminal extension
Function and mechanism
"SARS" and its enzyme product seryl-tRNA synthetase are involved in protein translation; specifically, seryl-tRNA synthetase catalyses the transfer of L-serine to tRNA (Ser). The cytosolic enzyme recognises its cognate tRNA species and binds with a high level of specificity, allowing the accurate interaction between corresponding codons and anticodons on mRNA and tRNA during protein translation.
Medical significance Pathogenic mutations are the cause of a condition with symptoms including developmental disabilities, seizures, and problems with muscle coordination (ataxia), which is called NEDMAS (Neurodevelopmental disorder with microcephaly, ataxia, and seizures).
See also Serine–tRNA ligase, mitochondrial (SARS2)
References
Further reading