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Glutamate-tRNA Ligase

Known as: Glu tRNA Ligase, Ligase, Glu-tRNA, Glutamyl T RNA Synthetase 
An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.
National Institutes of Health

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Papers overview

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Highly Cited
2013
Highly Cited
2013
Molecular mechanism of bacterial persistence by HipA.
HipA of Escherichia coli is a eukaryote-like serine-threonine kinase that inhibits cell growth and induces persistence (multidrug… Expand
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Highly Cited
2009
Highly Cited
2009
Dynamical networks in tRNA:protein complexes
Community network analysis derived from molecular dynamics simulations is used to identify and compare the signaling pathways in… Expand
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Highly Cited
2007
Highly Cited
2007
Identification and fine mapping of a thermo-sensitive chlorophyll deficient mutant in rice (Oryza sativa L.)
A thermo-sensitive chlorophyll deficient mutant was isolated from more than 15,000 transgenic rice lines. The mutant displayed… Expand
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Highly Cited
2003
Highly Cited
2003
ATP binding by glutamyl‐tRNA synthetase is switched to the productive mode by tRNA binding
Aminoacyl‐tRNA synthetases catalyze the formation of an aminoacyl‐AMP from an amino acid and ATP, prior to the aminoacyl transfer… Expand
Highly Cited
1998
Highly Cited
1998
Modular evolution of the Glx-tRNA synthetase family--rooting of the evolutionary tree between the bacteria and archaea/eukarya branches.
The accuracy of protein biosynthesis generally rests on a family of 20 aminoacyl-tRNA synthetases, one for each amino acid. In… Expand
Highly Cited
1998
Highly Cited
1998
Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis.
Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRNA) are essential components of protein synthesis. They can be formed by… Expand
Highly Cited
1996
Highly Cited
1996
The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl‐ and glutamyl‐tRNA synthetases.
Arc1p was found in a screen for components that interact genetically with Los1p, a nuclear pore‐associated yeast protein involved… Expand
Highly Cited
1995
Highly Cited
1995
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.
The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus… Expand
Highly Cited
1993
Highly Cited
1993
A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.
Early investigations into the interaction between Escherichia coli glutamyl-tRNA synthetase (GluRS) and tRNAGlu have implicated… Expand
Highly Cited
1986
Highly Cited
1986
A single glutamyl-tRNA synthetase aminoacylates tRNAGlu and tRNAGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNAGln1 in vitro.
In the presence or absence of its regulatory factor, the monomeric glutamyl-tRNA synthetase from Bacillus subtilis can… Expand
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