6.1.1.21: histidine-tRNA ligase
This is an abbreviated version!
For detailed information about histidine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.21
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6.1.1.21
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synthetases
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aminoacylation
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aminoacyl-trna
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autoantibody
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histidylation
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myositis
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anti-jo-1
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polymyositis
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anticodon
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dermatomyositis
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aarss
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perrault
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hiss
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histidinol
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anti-synthetase
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guanylyltransferase
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hsd17b4
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myositis-specific
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c10orf2
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thrrs
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threonyl-trna
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trna-like
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acid-starved
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seryl-trna
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analysis
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medicine
- 6.1.1.21
- synthetases
- aminoacylation
- aminoacyl-trna
- autoantibody
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histidylation
- myositis
-
anti-jo-1
- polymyositis
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anticodon
- dermatomyositis
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aarss
-
perrault
- hiss
- histidinol
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anti-synthetase
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guanylyltransferase
- hsd17b4
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myositis-specific
- c10orf2
- thrrs
- threonyl-trna
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trna-like
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acid-starved
- seryl-trna
- analysis
- medicine
Reaction
Synonyms
antihistidyl-tRNA synthetase, class II histidyl-tRNA synthetase, HARS, HARS1, HARS2, HisRS, HisRS-1, HisRS-2, Histidine translase, Histidine--tRNA ligase, Histidine--tRNA ligase homolog, histidine-tRNA ligase, histidine-tRNA ligase homolog, histidyl tRNA synthetase, Histidyl-transfer ribonucleate synthetase, histidyl-transfer RNA synthetase, Histidyl-tRNA synthetase, HRS, HTS1, Jo-1, Jo-1 antigen, mitochondrial histidyl tRNA synthetase, Synthetase, histidyl-transfer ribonucleate
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General Information
General Information on EC 6.1.1.21 - histidine-tRNA ligase
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evolution
malfunction
physiological function
additional information
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a conserved tRNA recognition pattern change during evolution leading to a divergent orthogonal HisRS/tRNAHis pair
evolution
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phylogenetic analysis reveals that tRNAThr1 originated from tRNAHis
evolution
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significantly different rate enhancements by four HisRS urzymes demonstrate that amino acid activation provides an experimental metric for recapitulating very early evolutionary events. Catalytic activities of HisRS-1 and HisRS-2 provide complementary support for Rodin-Ohno hypothesis that ancestral class I and II aaRS were encoded on opposite strands of same gene
evolution
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the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction emchanism, detailed overview
evolution
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the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction emchanism, detailed overview
evolution
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the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction mechanism, detailed overview
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mutations in the tRNAHis anticodon cause a drastic loss of in vitro histidylation, and mutations of bases A73 and U72 also reduce charging
malfunction
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the loss of fertility caused by hars-1 RNAi is partially mediated by apoptosis. Complete loss of hars-1 using the hars-1(tm4074) null allele. Homozygous hars-1 (tm4074) animals arrest development as L2 larvae, as determined by overall body size and by extent of gonad development, overview
malfunction
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mutations in histidyl-tRNA synthetase cause the dominant axonal peripheral neuropathy Charcot-Marie-Tooth disease type 2W
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hars-1 activity is required in Caenorhabditis elegans for fertility and proper germ cell development
physiological function
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mature tRNAHis has at its 5'-terminus an extra guanylate, designated as G-1. This is the major recognition element for HisRS to permit acylation of tRNAHis with histidine. However, recombinant HisRS allows complete histidylation of a Caulobacter crescentus tRNAHis transcript lacking G-1, and addition of G-1 does not improve the aminoacylation, but increases Km. The major recognition elements in Caulobacter crescentus tRNAHis are the anticodon, the discriminator base and U72, which are recognized by the divergent, based on sequence similarity, Caulobacter crescentus HisRS, a divergent orthogonal HisRS/tRNAHis pair
physiological function
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the enzyme induces muscle inflammation in B6.TLR2 and B6.TLR4 knockout mice. The enzyme induces interleukin 8 production in toll-like-receptor-transfected HEK-293 cells
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in idiopathic inflammatory myopathy, the aminoacyl-transfer RNA synthetases are targets of the autoimmune response. Among these antigens, antibodies against histidyl-transfer RNA synthetase are by far the most prominent found in 15-20% of myositis patients, and more strikingly, are detected in about 70% of patients with myositis and interstitial lung disease. Strong association of HisRS with interstitial lung disease in humans
additional information
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mouse HisRS without adjuvant, containing Toll-like receptor TLR-4, can induce sustained muscle inflammation and an adaptive immune response to HisRS. Mice lacking TLR-4 show that the ability of mouse HisRS to produce muscle inflammation does not require TLR-4 signaling, nor is it dependent on recognition of B cell and T cell receptors. When TLR-4-deficient animals are immunized with HisRS, they have a preserved inflammatory response in muscle but fail to generate a HisRS antibody response