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 in | Journal of molecular biology Vol. 361; no. 5; pp. 888 - 897 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.09.2006
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1016/j.jmb.2006.06.054 |