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Nucleic Acids Research Advance Access originally published online on December 23, 2007
Nucleic Acids Research 2008 36(4):1163-1175; doi:10.1093/nar/gkm1130
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Nucleic Acids Research, 2008, Vol. 36, No. 4 1163-1175
© 2007 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

Characterization of a ribonuclease III-like protein required for cleavage of the pre-rRNA in the 3'ETS in Arabidopsis

P. Comella, F. Pontvianne, S. Lahmy, F. Vignols, N. Barbezier, A. DeBures, E. Jobet, E. Brugidou, M. Echeverria and J. Sáez-Vásquez*

Laboratoire Génome et Développement des Plantes, UMR 5096 CNRS-UPVD-IRD, Université de Perpignan, 66860 Perpignan cedex, France

*To whom correspondence should be addressed. Tel: +33 4 68 66 21 32; Fax: +33 4 68 66 84 99; Email: saez{at}univ-perp.fr

Received September 6, 2007. Revised December 4, 2007. Accepted December 5, 2007.

Ribonuclease III (RNaseIII) is responsible for processing and maturation of RNA precursors into functional rRNA, mRNA and other small RNA. In contrast to bacterial and yeast cells, higher eukaryotes contain at least three classes of RNaseIII, including class IV or dicer-like proteins. Here, we describe the functional characterization of AtRTL2, an Arabidopsis thaliana RNaseIII-like protein that belongs to a small family of genes distinct from the dicer family. We demonstrate that AtRTL2 is required for 3'external transcribed spacer (ETS) cleavage of the pre-rRNA in vivo. AtRTL2 localizes in the nucleus and cytoplasm, a nuclear export signal (NES) in the N-terminal sequence probably controlling AtRTL2 cellular localization. The modeled 3D structure of the RNaseIII domain of AtRTL2 is similar to the bacterial RNaseIII domain, suggesting a comparable catalytic mechanism. However, unlike bacterial RNaseIII, the AtRTL2 protein forms a highly salt-resistant homodimer that is only disrupted on treatment with DTT. These data indicate that AtRTL2 may use a dimeric mechanism to cleave double-stranded RNA, but unlike bacterial or yeast RNase III proteins, AtRTL2 forms homodimers through formation of disulfide bonds, suggesting that redox conditions may operate to regulate the activity of RNaseIII.

Present addresses: Vignols F. and Brugidou C., IRD, Montpellier, France

Barbezier N., IGH/CNRS UPR 1142, Montpellier, France

The authors wish it to be known that, in their opinion, the first four authors should be regarded as joint First Authors.


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