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Published online 18 May 2004

Nucleic Acids Research, 2004, Vol. 32, No. 9 2768-2775
© 2004 Oxford University Press

A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon

Mickaël Blaise, Hubert Dominique Becker, Gérard Keith, Christian Cambillau1, Jacques Lapointe2, Richard Giegé and Daniel Kern*

Département ‘Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse’, UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 Rue René Descartes, F-67084 Strasbourg Cedex, France, 1 Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d’Aix-Marseille I et II, 31 Chemin J. Aiguier, F-13402 Marseille Cedex 20, France and 2 Département de Biochimie et Microbiologie, Faculté de Sciences et de Génie, CREFSIP, Université Laval, Québec, Canada G1K 7P4

*To whom correspondence should be addressed. Tel: +33 3 88 41 70 92; Fax: +33 3 88 60 22 18; Email: d.kern{at}ibmc.u-strasbg.fr
Correspondence may also be addressed to Richard Giegé. Tel: +33 3 88 70 58; Fax: +33 88 60 22 18; Email: r.giege{at}ibmc.u-strasbg.fr

Received April 15, 2004; Revised and Accepted April 22, 2004

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 tRNAAsp QUC anticodon. This conclusion is supported by a variety of biochemical data and by the inability of the enzyme to glutamylate tRNAAsp isolated from an E.coli tRNA-guanosine transglycosylase minus strain deprived of the capacity to exchange guanosine 34 with queuosine. Structural mimicry between the tRNAAsp anticodon stem and the tRNAGlu amino acid acceptor stem in prokaryotes encoding YadB proteins indicates that the function of these tRNA modifying enzymes, which we rename glutamyl-Q tRNAAsp synthetases, is conserved among prokaryotes.


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