Nucleic Acids Research Advance Access originally published online on October 29, 2006
Nucleic Acids Research 2006 34(21):6083-6094; doi:10.1093/nar/gkl622
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Nucleic Acids Research, 2006, Vol. 34, No. 21 6083-6094
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine
Département ‘Machineries traductionnelles’, UPR 9002 Architecture et Réactivité de l'ARN, Institut de Biologie Moléculaire et Cellulaire du CNRS 15, Rue René Descartes, F-67084 Strasbourg Cédex, France 1 Department of Biochemistry and Biotechnology, University of Thessaly 26 Ploutonos street, 41221 Larissa, Greece
*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
Received July 6, 2006. Revised August 8, 2006. Accepted August 8, 2006.
In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on tRNAAsn and tRNAGln. These pathways supply the deficiency of the organism in asparaginyl- and glutaminyl-tRNA synthtetases and provide the translational machinery with Asn-tRNAAsn and Gln-tRNAGln. So far, nothing is known about the structural elements that confer to tRNA the role of a specific cofactor in the formation of the cognate amino acid. We show herein, using aspartylated tRNAAsn and tRNAAsp variants, that amidation of Asp acylating tRNAAsn is promoted by the base pair U1–A72 whereas the G1–C72 pair and presence of the supernumerary nucleotide U20A in the D-loop of tRNAAsp prevent amidation. We predict, based on comparison of tRNAGln and tRNAGlu sequence alignments from bacteria using the AdT-dependent pathway to form Gln-tRNAGln, that the same combination of nucleotides also rules specific tRNA-dependent formation of Gln. In contrast, we show that the tRNA-dependent conversion of Asp into Asn by archaeal AdT is mainly mediated by nucleotides G46 and U47 of the variable region. In the light of these results we propose that bacterial and archaeal AdTs use kingdom-specific signals to catalyze the tRNA-dependent formations of Asn and Gln.
*Correspondence may also be addressed to Constantinos Stathopoulos. Tel: +30 2410 56 52 78; Fax: +30 2410 56 52 90; Email: cstath{at}bio.uth.gr
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