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

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...

Full description

Saved in:

Bibliographic Details
Published in:	Nucleic acids research Vol. 32; no. 9; pp. 2768 - 2775
Main Authors:	Blaise, Mickaël, Becker, Hubert Dominique, Keith, Gérard, Cambillau, Christian, Lapointe, Jacques, Giegé, Richard, Kern, Daniel
Format:	Journal Article
Language:	English
Published:	England Oxford University Press 01-01-2004 Oxford Publishing Limited (England)
Subjects:	Acylation Anticodon - chemistry Anticodon - genetics Anticodon - metabolism Base Sequence Biochemistry Biochemistry, Molecular Biology Biological Evolution Conserved Sequence Escherichia coli - enzymology Escherichia coli - genetics Glutamate-tRNA Ligase - chemistry Glutamate-tRNA Ligase - genetics Glutamate-tRNA Ligase - metabolism Life Sciences Molecular Mimicry Nucleoside Q - genetics Nucleoside Q - metabolism Periodic Acid - pharmacology RNA, Bacterial - chemistry RNA, Bacterial - genetics RNA, Bacterial - metabolism RNA, Transfer, Asp - chemistry RNA, Transfer, Asp - genetics RNA, Transfer, Asp - metabolism RNA, Transfer, Glu - chemistry RNA, Transfer, Glu - genetics RNA, Transfer, Glu - metabolism Structural Biology
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	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.
Bibliography:	To whom correspondence should be addressed. Tel: +33 3 88 41 70 92; Fax: +33 3 88 60 22 18; Email: d.kern@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@ibmc.u‐strasbg.fr ark:/67375/HXZ-JR8W25WJ-F Received April 15, 2004; Revised and Accepted April 22, 2004 local:gkh608 istex:8D5CF7D259FC1D41DA4B9A2DEE3488685F5CE689 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 PMCID: PMC419609 Correspondence may also be addressed to Richard Giegé. Tel: +33 3 88 70 58; Fax: +33 88 60 22 18; Email: r.giege@ibmc.u-strasbg.fr To whom correspondence should be addressed. Tel: +33 3 88 41 70 92; Fax: +33 3 88 60 22 18; Email: d.kern@ibmc.u-strasbg.fr
ISSN:	0305-1048 1362-4962 1362-4962
DOI:	10.1093/nar/gkh608