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Nucleic Acids Research Advance Access originally published online on January 12, 2009
Nucleic Acids Research 2009 37(4):1308-1322; doi:10.1093/nar/gkn1037
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Nucleic Acids Research, 2009, Vol. 37, No. 4 1308-1322
© 2009 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.

RNA

Deficiency of the tRNATyr:{Psi}35-synthase aPus7 in Archaea of the Sulfolobales order might be rescued by the H/ACA sRNA-guided machinery

Sébastien Muller1, Alan Urban1, Arnaud Hecker2, Fabrice Leclerc1, Christiane Branlant1,* and Yuri Motorin1

1Laboratoire de Maturation des ARN et Enzymologie Moléculaire, UMR 7567 CNRS-UHP Nancy Université, BP 239, 54506 Vandoeuvre-les-Nancy Cedex and 2Institut de Génétique et Microbiologie, Université Paris-Sud, IFR115, UMR8621-CNRS, 91405 Orsay, France

*To whom correspondence should be addressed. Tel: +33 3 83 68 43 03; Fax: +33 3 83 68 43 07; Email: christiane.branlant{at}maem.uhp-nancy.fr

Received August 10, 2008. Revised December 11, 2008. Accepted December 12, 2008.

Up to now, {Psi} formation in tRNAs was found to be catalysed by stand-alone enzymes. By computational analysis of archaeal genomes we detected putative H/ACA sRNAs, in four Sulfolobales species and in Aeropyrum pernix, that might guide {Psi}35 formation in pre-tRNATyr(GUA). This modification is achieved by Pus7p in eukarya. The validity of the computational predictions was verified by in vitro reconstitution of H/ACA sRNPs using the identified Sulfolobus solfataricus H/ACA sRNA. Comparison of Pus7-like enzymes encoded by archaeal genomes revealed amino acid substitutions in motifs IIIa and II in Sulfolobales and A. pernix Pus7-like enzymes. These conserved RNA:{Psi}-synthase- motifs are essential for catalysis. As expected, the recombinant Pyrococcus abyssi aPus7 was fully active and acted at positions 35 and 13 and other positions in tRNAs, while the recombinant S. solfataricus aPus7 was only found to have a poor activity at position 13. We showed that the presence of an A residue 3' to the target U residue is required for P. abyssi aPus7 activity, and that this is not the case for the reconstituted S. solfataricus H/ACA sRNP. In agreement with the possible formation of {Psi}35 in tRNATyr(GUA) by aPus7 in P. abyssi and by an H/ACA sRNP in S. solfataricus, the A36G mutation in the P. abyssi tRNATyr(GUA) abolished {Psi}35 formation when using P. abyssi extract, whereas the A36G substitution in the S. solfataricus pre-tRNATyr did not affect {Psi}35 formation in this RNA when using an S. solfataricus extract.


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