Publications
2004
Blaise M, Becker H D, Keith G, Cambillau C, Lapointe J, Giege R, Kern D
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon Article de journal
Dans: Nucleic Acids Res, vol. 32, no. 9, p. 2768-2775, 2004, ISBN: 15150343, (1362-4962 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Asp/chemistry/genetics/*metabolism RNA, Bacterial/chemistry/genetics/metabolism RNA, Glu/chemistry/genetics/metabolism Support, KERN Acylation Anticodon/chemistry/genetics/*metabolism Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics Evolution Glutamate-tRNA Ligase/*chemistry/genetics/*metabolism Molecular Mimicry Nucleoside Q/genetics/*metabolism Periodic Acid/pharmacology RNA, Non-U.S. Gov't, Transfer, Unité ARN
@article{,
title = {A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon},
author = {M Blaise and H D Becker and G Keith and C Cambillau and J Lapointe and R Giege and D Kern},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15150343},
isbn = {15150343},
year = {2004},
date = {2004-01-01},
journal = {Nucleic Acids Res},
volume = {32},
number = {9},
pages = {2768-2775},
abstract = {Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying enzyme that evidently glutamylates the queuosine residue, a modified nucleoside at the wobble position of the tRNA(Asp) QUC anticodon. This conclusion is supported by a variety of biochemical data and by the inability of the enzyme to glutamylate tRNA(Asp) isolated from an E.coli tRNA-guanosine transglycosylase minus strain deprived of the capacity to exchange guanosine 34 with queuosine. Structural mimicry between the tRNA(Asp) anticodon stem and the tRNA(Glu) amino acid acceptor stem in prokaryotes encoding YadB proteins indicates that the function of these tRNA modifying enzymes, which we rename glutamyl-Q tRNA(Asp) synthetases, is conserved among prokaryotes.},
note = {1362-4962
Journal Article},
keywords = {Asp/chemistry/genetics/*metabolism RNA, Bacterial/chemistry/genetics/metabolism RNA, Glu/chemistry/genetics/metabolism Support, KERN Acylation Anticodon/chemistry/genetics/*metabolism Base Sequence Conserved Sequence Escherichia coli/*enzymology/*genetics Evolution Glutamate-tRNA Ligase/*chemistry/genetics/*metabolism Molecular Mimicry Nucleoside Q/genetics/*metabolism Periodic Acid/pharmacology RNA, Non-U.S. Gov't, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}