Nucleic Acids Research Advance Access published online on August 18, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl530
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© 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-commerical use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Formation of the conserved pseudouridine at position 55 in archaeal tRNA
Institut de Recherches Microbiologiques J.-M. Wiame, Avenue E. Gryson 1 B-1070 Bruxelles, Belgium 1 Department of Biochemistry and Molecular Biology, University of Georgia Life Sciences Building, Athens, GA 30602, USA 2 Department of Genetics, University of Georgia Life Sciences Building, Athens, GA 30602, USA 3 Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique Avenue de la Terrasse 1, F-91198 Gif-sur-Yvette, France 4 Laboratoire de Microbiologie, Université Libre de Bruxelles Institut de Recherches Microbiologiques J.-M. Wiame, Avenue E. Gryson 1, B-1070 Bruxelles, Belgium
*To whom correspondence should be addressed. Tel: +32 2 526 72 83; Fax: +32 2 526 72 73; Email: ldroogma{at}ulb.ac.be
Received June 6, 2006. Revised July 10, 2006. Accepted July 10, 2006.
Pseudouridine (
) located at position 55 in tRNA is a nearly universally conserved RNA modification found in all three domains of life. This modification is catalyzed by TruB in bacteria and by Pus4 in eukaryotes, but so far the 55 synthase has not been identified in archaea. In this work, we report the ability of two distinct pseudouridine synthases from the hyperthermophilic archaeon Pyrococcus furiosus to specifically modify U55 in tRNA in vitro. These enzymes are pfuCbf5, a protein known to play a role in RNA-guided modification of rRNA, and pfuPsuX, a previously uncharacterized enzyme that is not a member of the TruB/Pus4/Cbf5 family of pseudouridine synthases. pfuPsuX is hereafter renamed pfuPus10. Both enzymes specifically modify tRNA U55 in vitro but exhibit differences in substrate recognition. In addition, we find that in a heterologous in vivo system, pfuPus10 efficiently complements an Escherichia coli strain deficient in the bacterial 55 synthase TruB. These results indicate that it is probable that pfuCbf5 or pfuPus10 (or both) is responsible for the introduction of pseudouridine at U55 in tRNAs in archaea. While we cannot unequivocally assign the function from our results, both possibilities represent unexpected functions of these proteins as discussed herein.
*Correspondence may also be addressed to Rebecca M. Terns. Tel: +1 706 542 1703; Fax: +1 706 542 1752; Email: rterns{at}bmb.uga.edu
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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