Crystal Structure of a Non-discriminating Glutamyl-tRNA Synthetase

Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA Gln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS)....

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Published inJournal of molecular biology Vol. 361; no. 5; pp. 888 - 897
Main Authors Schulze, Jörg O., Masoumi, Ava, Nickel, Daniel, Jahn, Martina, Jahn, Dieter, Schubert, Wolf-Dieter, Heinz, Dirk W.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.09.2006
Subjects
Amino Acid Sequence
aminoacylation
Anticodon - metabolism
anticodon recognition
Binding Sites
Catalysis
Crystallography, X-Ray
Cyanobacteria - enzymology
Glutamate-tRNA Ligase - chemistry
Glutamic Acid - metabolism
glutaminyl-tRNA synthetase
misacylation
mischarging
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Structure, Tertiary
Thermosynechococcus elongatus
Thermus thermophilus
D
Tth
CP
AdT
Eco
SC
misacylation
glutaminyl-tRNA synthetase
ND
anticodon recognition
Tel
aminoacylation
mischarging
AARS
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Abstract Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA Gln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA Glu and tRNA Gln with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA Glu. Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS Tel ) in complex with glutamate at a resolution of 2.45 Å. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS Tth ). We confirm experimentally that GluRS Tel is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA Glu and of Glu-tRNA Gln. Anticodons of tRNA Glu ( 34C/UUC 36) and tRNA Gln ( 34C/UUG 36) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS Tth by the residue Arg358. In ND-GluRS Tel this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA Gln to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.
AbstractList Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA(Gln) is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA(Glu) and tRNA(Gln) with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA(Glu). Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS(Tel)) in complex with glutamate at a resolution of 2.45 A. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS(Tth)). We confirm experimentally that GluRS(Tel) is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA(Glu) and of Glu-tRNA(Gln). Anticodons of tRNA(Glu) (34C/UUC36) and tRNA(Gln) (34C/UUG36) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS(Tth) by the residue Arg358. In ND-GluRS(Tel) this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA(Gln) to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.
Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA Gln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA Glu and tRNA Gln with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA Glu. Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS Tel ) in complex with glutamate at a resolution of 2.45 Å. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS Tth ). We confirm experimentally that GluRS Tel is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA Glu and of Glu-tRNA Gln. Anticodons of tRNA Glu ( 34C/UUC 36) and tRNA Gln ( 34C/UUG 36) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS Tth by the residue Arg358. In ND-GluRS Tel this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA Gln to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.
Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA super(G) super(l) super(n) is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA super(G) super(l) super(u) and tRNA super(G) super(l) super(n) with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA super(G) super(l) super(u). Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS sub(T) sub(e) sub(l)) in complex with glutamate at a resolution of 2.45 A. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS sub(T) sub(t) sub(h)). We confirm experimentally that GluRS sub(T) sub(e) sub(l) is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA super(G) super(l) super(u) and of Glu-tRNA super(G) super(l) super(n). Anticodons of tRNA super(G) super(l) super(u) ( super(3) super(4)C/UUC super(3) super(6)) and tRNA super(G) super(l) super(n) ( super(3) super(4)C/UUG super(3) super(6)) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS sub(T) sub(t) sub(h) by the residue Arg358. In ND-GluRS sub(T) sub(e) sub(l) this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA super(G) super(l) super(n) to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.
Author Schubert, Wolf-Dieter
Heinz, Dirk W.
Jahn, Martina
Jahn, Dieter
Schulze, Jörg O.
Masoumi, Ava
Nickel, Daniel
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  givenname: Martina
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  givenname: Dirk W.
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  email: Dirk.Heinz@gbf.de
  organization: Division of Structural Biology, German Research Centre for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany
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Keywords D
Tth
CP
AdT
Eco
SC
misacylation
glutaminyl-tRNA synthetase
ND
anticodon recognition
Tel
aminoacylation
mischarging
AARS
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Snippet Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA...
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SubjectTerms Amino Acid Sequence
aminoacylation
Anticodon - metabolism
anticodon recognition
Binding Sites
Catalysis
Crystallography, X-Ray
Cyanobacteria - enzymology
Glutamate-tRNA Ligase - chemistry
Glutamic Acid - metabolism
glutaminyl-tRNA synthetase
misacylation
mischarging
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Structure, Tertiary
Thermosynechococcus elongatus
Thermus thermophilus
Title Crystal Structure of a Non-discriminating Glutamyl-tRNA Synthetase
URI https://dx.doi.org/10.1016/j.jmb.2006.06.054
https://www.ncbi.nlm.nih.gov/pubmed/16876193
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https://search.proquest.com/docview/68748610
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