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Queuine tRNA-ribosyltransferase 1

tRNA-guanine transglycosylase, TGT TGT
This gene encodes the catalytic subunit of tRNA-guanine transglycosylase. tRNA-guanine transglycosylase is a heterodimeric enzyme complex that plays a critical role in tRNA modification by synthesizing the 7-deazaguanosine queuosine, which is found in tRNAs that code for asparagine, aspartic acid, histidine and tyrosine. A pseudogene of this gene is located on the long arm of chromosome X. [provided by RefSeq, Feb 2012] (from NCBI)
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Papers on tRNA-guanine transglycosylase
Horizontal gene transfer of a Chlamydial tRNA-guanine transglycosylase gene to eukaryotic microbes.
Harman et al., Melbourne, Australia. In Mol Phylogenet Evol, Jan 2016
Given that the S. flexneri tRNA-guanine transglycosylase can be targeted by drugs, we propose that the bacterial-like tRNA-guanine transglycosylases could potentially be targeted in a similar fashion in pathogenic amoebae that possess these enzymes such as Acanthamoeba castellanii.
Multisite-specific archaeosine tRNA-guanine transglycosylase (ArcTGT) from Thermoplasma acidophilum, a thermo-acidophilic archaeon.
Hori et al., Japan. In Nucleic Acids Res, Jan 2016
UNASSIGNED: Archaeosine (G(+)), which is found only at position 15 in many archaeal tRNA, is formed by two steps, the replacement of the guanine base with preQ0 by archaeosine tRNA-guanine transglycosylase (ArcTGT) and the subsequent modification of preQ0 to G(+) by archaeosine synthase.
Dynamic modulation of Dnmt2-dependent tRNA methylation by the micronutrient queuine.
Ehrenhofer-Murray et al., Berlin, Germany. In Nucleic Acids Res, Jan 2016
In vivo tRNA methylation levels were stimulated by growth of cells in queuine-containing medium; in vitro Pmt1 activity was enhanced on Q-containing RNA; and queuine-stimulated in vivo methylation was abrogated by the absence of the enzyme that inserts queuine into tRNA, eukaryotic tRNA-guanine transglycosylase.
Correlation between the stability of tRNA tertiary structure and the catalytic efficiency of a tRNA-modifying enzyme, archaeal tRNA-guanine transglycosylase.
Yokogawa et al., Gifu, Japan. In Genes Cells, Jan 2016
During archaeosine biosynthesis, archaeal tRNA-guanine transglycosylase (ArcTGT) first replaces the guanine base at position 15 with 7-cyano-7-deazaguanine (preQ0 ).
What Glues a Homodimer Together: Systematic Analysis of the Stabilizing Effect of an Aromatic Hot Spot in the Protein-Protein Interface of the tRNA-Modifying Enzyme Tgt.
Klebe et al., Marburg an der Lahn, Germany. In Acs Chem Biol, Sep 2015
A null mutation in the tgt gene encoding the tRNA-modifying enzyme tRNA-guanine transglycosylase (Tgt) was found to drastically decrease the pathogenicity of Shigella bacteria, suggesting the use of Tgt as putative target for selective antibiotics.
Replacement of water molecules in a phosphate binding site by furanoside-appended lin-benzoguanine ligands of tRNA-guanine transglycosylase (TGT).
Diederich et al., Zürich, Switzerland. In Chemistry, Feb 2015
The enzyme tRNA-guanine transglycosylase has been identified as a drug target for the foodborne illness shigellosis.
Identification of Plasmodium falciparum apicoplast-targeted tRNA-guanine transglycosylase and its potential inhibitors using comparative genomics, molecular modelling, docking and simulation studies.
Ranjan et al., Hyderābād, India. In J Biomol Struct Dyn, 2014
Through sequence comparison and phylogenetic analysis, we have identified P. falciparum apicoplast tRNA-guanine 34 transglycosylase (TGT, EC:, which shows evidence of its prokaryotic origin.
Adenosylmethionine decarboxylase 1 (AMD1)-mediated mRNA processing and cell adhesion activated & inhibited transition mechanisms by different comparisons between chimpanzee and human left hemisphere.
Feng et al., Beijing, China. In Cell Biochem Biophys, 2014
As visualized by GO, KEGG, GenMAPP, BioCarta, and disease database integration, we proposed mainly that AMD1-stimulated different complete network was involved in AMD1 activation with cytoplasm ubiquitin specific peptidase (tRNA-guanine transglycosylase) to nucleus paired box-induced mRNA processing, whereas the corresponding inhibited network participated in AMD1 repression with cytoplasm protocadherin gamma and adaptor-related protein complex 3-induced cell adhesion in lower chimpanzee left hemisphere.
Impact of protein and ligand impurities on ITC-derived protein-ligand thermodynamics.
Klebe et al., Marburg an der Lahn, Germany. In Biochim Biophys Acta, 2014
RESULTS AND CONCLUSIONS: We used trypsin and tRNA-guanine transglycosylase (TGT), together with high affinity ligands to investigate the effect of errors in protein concentration as well as the impact of ligand impurities on the apparent thermodynamics.
Beyond affinity: enthalpy-entropy factorization unravels complexity of a flat structure-activity relationship for inhibition of a tRNA-modifying enzyme.
Klebe et al., Marburg an der Lahn, Germany. In J Med Chem, 2014
We investigated the thermodynamic signature of two classes of lin-benzopurines binding to tRNA-guanine transglycosylase.
Chasing protons: how isothermal titration calorimetry, mutagenesis, and pKa calculations trace the locus of charge in ligand binding to a tRNA-binding enzyme.
Klebe et al., Marburg an der Lahn, Germany. In J Med Chem, 2014
We investigated the protonation inventory in a series of lin-benzoguanines binding to tRNA-guanine transglycosylase, showing pronounced buffer dependency during ITC measurements.
High-affinity inhibitors of Zymomonas mobilis tRNA-guanine transglycosylase through convergent optimization.
Diederich et al., Zürich, Switzerland. In Acta Crystallogr D Biol Crystallogr, 2013
The tRNA-modifying enzyme tRNA-guanine transglycosylase (TGT) has been recognized as a drug target for the treatment of the foodborne illness shigellosis.
Differential heterocyclic substrate recognition by, and pteridine inhibition of E. coli and human tRNA-guanine transglycosylases.
Garcia et al., Ann Arbor, United States. In Biochem Biophys Res Commun, 2011
the inhibition of the human TGT by biopterin, consistent with earlier reports on other eukaryal TGTs, and supportive of the concept that pteridines may regulate eukaryal TGT activity in vivo.
Evolution of eukaryal tRNA-guanine transglycosylase: insight gained from the heterocyclic substrate recognition by the wild-type and mutant human and Escherichia coli tRNA-guanine transglycosylases.
Garcia et al., Ann Arbor, United States. In Nucleic Acids Res, 2011
phylogenetic and kinetic analyses support the conclusion that all tRNA-guanine transglycosylases have divergently evolved to specifically recognize their cognate heterocyclic substrates.
Characterization of the human tRNA-guanine transglycosylase: confirmation of the heterodimeric subunit structure.
Garcia et al., Ann Arbor, United States. In Rna, 2010
TGT is composed of a catalytic subunit, QTRT1, and QTRTD1, not USP14. QTRTD1 has been implicated as the salvage enzyme that generates free queuine from QMP.
Probing the intermediacy of covalent RNA enzyme complexes in RNA modification enzymes.
Garcia et al., Ann Arbor, United States. In Methods Enzymol, 2006
As a case study for the proof of intermediacy, we report the use of this gel-shift assay under mildly denaturing conditions to probe the kinetic competency of the covalent association between RNA and the tRNA modifying enzyme tRNA-guanine transglycosylase (TGT).
Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme.
Yokoyama et al., Tokyo, Japan. In Cell, 2003
In this study, we determined the crystal structure of tRNA bound with archaeosine tRNA-guanine transglycosylase, which modifies G15 of the D arm in the core.
Biosynthesis of the 7-deazaguanosine hypermodified nucleosides of transfer RNA.
Iwata-Reuyl, Portland, United States. In Bioorg Chem, 2003
This review covers current understanding of the physiology and biosynthesis of these remarkable nucleosides, with particular emphasis on the only two enzymes that have been discovered in the pathways: tRNA-guanine transglycosylase (TGT), which catalyzes the insertion of a modified base into the polynucleotide with the concomitant elimination of the genetically encoded guanine in the biosynthesis of both nucleosides, and S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA), which catalyzes the penultimate step in the biosynthesis of queuosine, the construction of the carbocyclic side chain.
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