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Nucleic Acids Research 2006 34(3):826-839; doi:10.1093/nar/gkj482
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Published online 2 February 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5–aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity

Xavier Manival, Christophe Charron, Jean-Baptiste Fourmann, François Godard, Bruno Charpentier* and Christiane Branlant

Laboratoire de Maturation des ARN et Enzymologie Moléculaire, UMR 7567 UHP-CNRS, Université des Sciences et Techniques Henri Poincaré Nancy I 54506 Vandoeuvre-Lès-Nancy cedex, France

*To whom correspondence should be addressed. Tel: +33 3 83 68 43 16; Fax: +33 3 83 68 43 07; Email: bruno.charpentier{at}maem.uhp-nancy.fr

Received December 8, 2005. Revised January 14, 2006. Accepted January 14, 2006.

In archaeal rRNAs, the isomerization of uridine into pseudouridine ({Psi}) is achieved by the H/ACA sRNPs and the minimal set of proteins required for RNA:{Psi}-synthase activity is the aCBF5–aNOP10 protein pair. The crystal structure of the aCBF5–aNOP10 heterodimer from Pyrococcus abyssi was solved at 2.1 Å resolution. In this structure, protein aNOP10 has an extended shape, with a zinc-binding motif at the N-terminus and an {alpha}-helix at the C-terminus. Both motifs contact the aCBF5 catalytic domain. Although less efficiently as does the full-length aNOP10, the aNOP10 C-terminal domain binds aCBF5 and stimulates the RNA-guided activity. We show that the C-terminal domain of aCBF5 (the PUA domain), which is wrapped by an N-terminal extension of aCBF5, plays a crucial role for aCBF5 binding to the guide sRNA. Addition of this domain in trans partially complement particles assembled with an aCBF5{Delta}PUA truncated protein. In the crystal structure, the aCBF5–aNOP10 complex forms two kinds of heterotetramers with parallel and perpendicular orientations of the aNOP10 terminal {alpha}-helices, respectively. By gel filtration assay, we showed that aNOP10 can dimerize in solution. As both residues Y41 and L48 were needed for dimerization, the dimerization likely takes place by interaction of parallel {alpha}-helices.

Present address: François Godard, Institut de Biochimie et de Génétique Cellulaire (IBGC), UMR5095 Université Bordeaux2- CNRS, 1 rue Camille Saint-Saens, 33077 Bordeaux cedex, France

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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