IARS1
IARS1 (isoleucyl-tRNA synthetase 1, also known as ILRS or IARS) is the cytoplasmic isoleucine--tRNA ligase. It catalyses the attachment of isoleucine to its cognate tRNA, a core step in linking amino acids to the nucleotide triplets of the genetic code. Browse Assay Genie's current range of IARS1 research reagents below, or read on for the biology behind the target.
IARS1 belongs to the class-I aminoacyl-tRNA synthetase family. Like other members, it catalyses the specific attachment of an amino acid to its cognate tRNA in a two-step reaction. The amino acid is first activated by ATP to form an aminoacyl-AMP intermediate, and is then transferred to the acceptor end of the tRNA. In the case of IARS1, the amino acid is isoleucine. The enzyme is classified as EC 6.1.1.5 and is found in the cytoplasm, including the cytosol.
Aminoacyl-tRNA synthetases carry out the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with the nucleotide triplets contained in tRNAs, these enzymes are thought to be among the first proteins that appeared in evolution. The IARS1 gene is a member of the HGNC group of class I aminoacyl tRNA synthetases. It is also listed among the microRNA protein coding host genes and the small nucleolar RNA protein coding host genes. Alternatively spliced transcript variants have been found for the gene.
The gene was previously named isoleucyl-tRNA synthetase, and the symbols ILRS and IARS appear in older literature. Isoleucine-tRNA synthetase has been identified as a target of autoantibodies in the autoimmune disease polymyositis/dermatomyositis, which links this housekeeping enzyme to autoimmunity research. A mouse ortholog, Iars1, is recognised, which supports comparative and model-organism work on the protein.
IARS1 performs the two-step aminoacylation of tRNA with isoleucine, making it a reference enzyme for studying how amino acids are matched to tRNAs.
Isoleucine-tRNA synthetase is a target of autoantibodies in polymyositis/dermatomyositis, so IARS1 is relevant to studies of autoantigens in this disease.
As a class-I aminoacyl-tRNA synthetase, IARS1 is used in comparative work on proteins thought to be among the earliest to appear in evolution.
The IARS1 gene produces alternatively spliced transcript variants and hosts microRNA and snoRNA genes, offering topics for gene regulation studies.
IARS1 is the cytoplasmic isoleucine--tRNA ligase. It catalyses a two-step reaction in which isoleucine is activated by ATP to form an aminoacyl-AMP intermediate and then transferred to the acceptor end of its cognate tRNA, linking amino acids to the genetic code.
IARS1 is also known as ILRS and IARS, and its earlier name was isoleucyl-tRNA synthetase. UniProt lists the protein as isoleucine--tRNA ligase, cytoplasmic. The enzyme is classified as EC 6.1.1.5, and alternatively spliced transcript variants have been reported for the gene.
Isoleucine-tRNA synthetase is a target of autoantibodies in polymyositis/dermatomyositis. The gene has a mouse ortholog, Iars1. Aminoacyl-tRNA synthetases are thought to be among the earliest proteins in evolution; check the datasheet of any product for its validated reactivity.
Other aminoacyl-tRNA synthetases and translation-related enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P41252; product specifications from Assay Genie datasheets.