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GLN4 Gln4p

glutaminyl-tRNA synthetase, GlnRS
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. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, STEP, V1a, SET
Papers on glutaminyl-tRNA synthetase
Partial suppression of the respiratory defect of qrs1/her2 glutamyl-tRNA amidotransferase mutants by overexpression of the mitochondrial pentatricopeptide Msc6p.
Barros et al., São Paulo, Brazil. In Curr Genet, Feb 2016
This is an essential step in mitochondrial translation because of the lack of a specific mitochondrial aminoacyl glutaminyl-tRNA synthetase.
Calpain Cleaves Most Components in the Multiple Aminoacyl-tRNA Synthetase Complex and Affects Their Functions.
Wang et al., Shanghai, China. In J Biol Chem, Nov 2015
The cleavage sites of calpain in ArgRS, GlnRS, and p43 were precisely mapped.
Recombinant expression, purification, and crystallization of the glutaminyl-tRNA synthetase from Toxoplasma gondii.
Belrhali et al., Grenoble, France. In Protein Expr Purif, Jun 2015
Because no structural data currently exists for a protozoan glutaminyl-tRNA synthetase (QRS), an understanding of its potential as a drug target and its function in the assembly of the Toxoplasma multi-aminoacyl tRNA (MARS) complex is therefore lacking.
Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase.
Basu et al., Calcutta, India. In Biosci Rep, 2014
From extensive structural and sequence analyses from whole genome database of bacterial GluRS, we further show that in addition to many bacterial GluRS lacking a zinc-binding motif, the pZBD is actually deleted in some bacteria, all containing either glutaminyl-tRNA synthetase (GlnRS) or a second copy of GluRS (GluRS2).
Architecture and metamorphosis.
Yang et al., Jupiter, United States. In Top Curr Chem, 2013
The human MSC consists of nine aaRSs (LysRS, ArgRS, GlnRS, AspRS, MetRS, IleRS, LeuRS, GluProRS, and bifunctional aaRs) and three scaffold proteins (AIMP1/p43, AIMP2/p38, and AIMP3/p18), and has a molecular weight of 1.5 million Dalton.
Aminoacyl-tRNA Synthetases in the Bacterial World.
Springer et al., In Ecosal Plus, 2012
AaRSs show hugestructural plasticity related to function andlimited idiosyncrasies that are kingdom or even speciesspecific (e.g.,the presence in many Bacteria of non discriminating aaRSs compensating for the absence of one or two specific aaRSs, notably AsnRS and/or GlnRS).Diversity, as well, occurs in the mechanisms of aaRS gene regulation that are not conserved in evolution, notably betweendistant groups such as Gram-positive and Gram-negative Bacteria.Thereview focuses on bacterial aaRSs (and their paralogs) and covers their structure, function, regulation,and evolution.
Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase.
Grayhack et al., Buffalo, United States. In Nucleic Acids Res, 2012
A functional and structural analysis of the N-terminal appended domain of Saccharomyces cerevisiae GlnRS, Gln4.
Translating organellar glutamine codons: a case by case scenario?
Becker et al., Strasbourg, France. In Rna Biol, 2009
All eukaryotic genomes sequenced so far, display a single glutaminyl-tRNA synthetase (QRS) gene which is at least responsible for the cytosolic QRS activity, as well as a gene coding for a mitochondrial ortholog of the essential GatB subunit of the tRNA-dependent amidotransferase (AdT).
Stressing out over survival: glutamine as an apoptotic modulator.
Bode et al., Saint Louis, United States. In J Surg Res, 2006
To date, GLN transporters, cellular hydration, glutaminyl-tRNA synthetase, ATP levels, mRNA stability, and glutathione economy have been variably implicated in GLN-dependent survival signaling.
Domain-specific recruitment of amide amino acids for protein synthesis.
Söll et al., New Haven, United States. In Nature, 2000
These amide aminoacyl-tRNAs can be formed by the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, respectively.
Glutamyl-tRNA sythetase.
Lapointe et al., Göttingen, Germany. In Biol Chem, 1997
Glutamyl-tRNA synthetase (GluRS) belongs to the class I aminoacyl-tRNA synthetases and shows several similarities with glutaminyl-tRNA synthetase concerning structure and catalytic properties.
Glutaminyl-tRNA synthetase.
Söll et al., Göttingen, Germany. In Biol Chem, 1997
Among the twenty aminoacyl-tRNA synthetases glutaminyl-tRNA synthetase occupies a special position: it is one of only two enzymes of this family which is not found in all organisms, being mainly absent from gram positive eubacteria, archaebacteria and organelles.
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.
Morikawa et al., Tokyo, Japan. In Science, 1995
The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain.
Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase.
Moras et al., Strasbourg, France. In Nature, 1993
The five aminoacyl-tRNA synthetases whose crystal structures are known (MetRS, TyrRS and GlnRS in class I, SerRS and AspRS in class II) belong to different subgroups.
Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes.
Söll et al., New Haven, United States. In Science, 1990
These genetic experiments define two positions in GlnRS where amino acid substitution results in a relaxed specificity of tRNA discrimination.
Protein biosynthesis in organelles requires misaminoacylation of tRNA.
Söll et al., New Haven, United States. In Nature, 1988
Aminoacylation studies show that chloroplasts, plant and animal mitochondria, as well as cyanobacteria, lack any detectable glutaminyl-tRNA synthetase activity.
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