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EMBO reports 4, 12, 1150–1155 (2003)
doi:10.1038/sj.embor.7400020
Published online: 14 November 2003
X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex
Stéphane Thore1, 3, Fabienne Mauxion2, 4, Bertrand Séraphin2, 4 & Dietrich Suck1, 3
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1 European Molecular Biology Laboratory,
Heidelberg, Germany
2 Equipe Labelisée La Ligue, Centre de
Génétique Moléculaire, Gif sur Yvette
Cedex, France
3 European Molecular Biology Laboratory,
Meyerhofstrasse 1, D-69117 Heidelberg,
Germany
4 Equipe Labelisée La Ligue, Centre de
Génétique Moléculaire, CNRS UPR2167, Avenue
de la Terrasse, 91198 Gif sur Yvette Cedex,
France
To whom correspondence should be addressed
Dietrich Suck Tel: +49 6221 387 307; Fax: +49 6221 387 306;
E-mail: suck@embl-heidelberg.de
Received 22 August 2003; Accepted 19 September 2003; Published online 14 November 2003.
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Abstract
In Saccharomyces cerevisiae, a large complex, known as the
Ccr4–Not complex, containing two nucleases, is responsible for mRNA
deadenylation. One of these nucleases is called Pop2 and has been identified by
similarity with PARN, a human poly(A) nuclease. Here, we present the crystal
structure of the nuclease domain of Pop2 at 2.3 Å resolution. The domain
has the fold of the DnaQ family and represents the first structure of an RNase
from the DEDD superfamily. Despite the presence of two non-canonical residues
in the active site, the domain displays RNase activity on a broad range of RNA
substrates. Site-directed mutagenesis of active-site residues demonstrates the
intrinsic ability of the Pop2 RNase D domain to digest RNA. This first
structure of a nuclease involved in the 3'–5' deadenylation
of mRNA in yeast provides information for the understanding of the mechanism by
which the Ccr4–Not complex achieves its functions.
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