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Isoleucyl-tRNA synthetase

isoleucyl-tRNA synthetase, Isoleucine-tRNA Ligase
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAS, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Isoleucine-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family and has been identified as a target of autoantibodies in the autoimmune disease polymyositis/dermatomyositis. Two alternatively spliced variants have been isolated that represent alternate 5' UTRs. [provided by RefSeq, Jul 2008] (from NCBI)
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Papers on isoleucyl-tRNA synthetase
A novel therapeutic target for peripheral nerve injury-related diseases: aminoacyl-tRNA synthetases.
Jeong et al., Seoul, South Korea. In Neural Regen Res, Oct 2015
Of 20 AminoARSs, we found that phenylalanyl-tRNA synthetase beta chain (FARSB), isoleucyl-tRNA synthetase (IARS) and methionyl-tRNA synthetase (MARS) mRNA expression was increased in spinal dorsal horn neurons on the injured side, but not in glial cells.
The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase.
Gruic-Sovulj et al., Zagreb, Croatia. In J Biol Chem, Jun 2015
Escherichia coli isoleucyl-tRNA synthetase (IleRS) exploits both the tRNA-dependent pre- and post-transfer editing pathways to minimize errors in translation.
Juvenile polymyositis associated with anti-OJ (anti-isoleucyl-tRNA synthetase) autoantibody in a 13-year-old girl.
Mimori et al., Yao, Japan. In Mod Rheumatol, Apr 2015
UNASSIGNED: A 13-year-old girl was admitted for persistent thigh pain and remittent fever and was diagnosed as having juvenile polymyositis.
T box riboswitches in Actinobacteria: translational regulation via novel tRNA interactions.
Henkin et al., Columbus, United States. In Proc Natl Acad Sci U S A, Feb 2015
In this study, a novel group of isoleucyl-tRNA synthetase gene (ileS) T box leader sequences found in organisms of the phylum Actinobacteria was investigated.
Structure-function analyses of cytochrome P450revI involved in reveromycin A biosynthesis and evaluation of the biological activity of its substrate, reveromycin T.
Osada et al., Saitama, Japan. In J Biol Chem, 2014
Our results show that RM-T had stronger anticancer activity and isoleucyl-tRNA synthetase inhibition than RM-A.
Mutation in the nuclear-encoded mitochondrial isoleucyl-tRNA synthetase IARS2 in patients with cataracts, growth hormone deficiency with short stature, partial sensorineural deafness, and peripheral neuropathy or with Leigh syndrome.
Samuels et al., Montréal, Canada. In Hum Mutat, 2014
Using SNP genotyping and whole-exome sequencing, we identified a single likely causal variant, a missense mutation in a conserved residue of the nuclear gene IARS2, encoding mitochondrial isoleucyl-tRNA synthetase.
Determinants for tRNA-dependent pretransfer editing in the synthetic site of isoleucyl-tRNA synthetase.
Gruic-Sovulj et al., Zagreb, Croatia. In Biochemistry, 2014
Escherichia coli isoleucyl-tRNA synthetase (EcIleRS) is a class I aaRS that is notable for its use of tRNA-dependent pretransfer editing to hydrolyze noncognate valyl-adenylate prior to aminoacyl-tRNA formation.
Relaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetases.
Ibba et al., Columbus, United States. In Mbio, 2013
To investigate the extent of tRNA mischarging in this pathogen, the aminoacylation profiles of class I isoleucyl-tRNA synthetase (IleRS) and class II lysyl-tRNA synthetase (LysRS) were determined.
Clinical relevance of mupirocin resistance in Staphylococcus aureus.
Bonten et al., Utrecht, Netherlands. In J Hosp Infect, 2013
Mupirocin prevents bacterial protein synthesis by inhibiting the bacterial isoleucyl-tRNA synthetase (IleRS).
Aminoacyl-tRNA synthetase inhibitors as potent antibacterials.
Zhu et al., Nanjing, China. In Curr Med Chem, 2011
In this review, we examine the latest developments and structure-activity relationship (SAR) analysis of aminoacyl-tRNA synthetases inhibitors, including methionyl-tRNA synthetase, isoleucyl-tRNA synthetase and phenylalanyl-tRNA synthetase inhibitors.
Mupirocin: biosynthesis, special features and applications of an antibiotic from a gram-negative bacterium.
Thomas et al., Birmingham, United Kingdom. In Appl Microbiol Biotechnol, 2011
Mupirocin inhibits isoleucyl-tRNA synthetase and has been used since 1985 to help prevent infection by methicillin-resistant Staphylococcus aureus, particularly within hospitals.
Resistance to and synthesis of the antibiotic mupirocin.
Simpson et al., Birmingham, United Kingdom. In Nat Rev Microbiol, 2010
Low-level resistance to the antibiotic arises by mutation of the mupirocin target, isoleucyl-tRNA synthetase, whereas high-level resistance is due to the presence of an isoleucyl-tRNA synthetase with many similarities to eukaryotic enzymes.
Finding of an isoleucine derivative of a recombinant protein for pharmaceutical use.
Hayashi et al., Toda, Japan. In J Pharm Biomed Anal, 2003
We, therefore, propose that betaMeNle is biosynthesized by E. coli, activated by E. coli isoleucyl-tRNA synthetase (IleRS), then incorporated into the overproduced recombinant hirudin analog.
Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide.
Schimmel et al., Cambridge, United States. In Science, 1995
When the hybrid sequence was transplanted into isoleucyl-tRNA synthetase, active enzyme was generated in vivo and in vitro.
Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase.
Schimmel et al., In Science, 1985
The entire 939-amino acid primary structure of Escherichia coli isoleucyl-tRNA synthetase is now reported.
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