Article abstract
Nature Structural & Molecular Biology 14, 15 - 22 (2007)
Published online: 17 December 2006 | doi:10.1038/nsmb1184
A single subunit, Dis3, is essentially responsible for yeast exosome core activity
Andrzej Dziembowski1,3, Esben Lorentzen2, Elena Conti2,4 & Bertrand Séraphin1
Abstract
The conserved core of the exosome, the major eukaryotic 3' 
5' exonuclease, contains nine subunits that form a ring similar to the phosphorolytic bacterial PNPase and archaeal exosome, as well as Dis3. Dis3 is homologous to bacterial RNase II, a hydrolytic enzyme. Previous studies have suggested that all subunits are active 3' 5' exoRNases. We show here that Dis3 is responsible for exosome core activity. The purified exosome core has a hydrolytic, processive and Mg2+-dependent activity with characteristics similar to those of recombinant Dis3. Moreover, a catalytically inactive Dis3 mutant has no exosome core activity in vitro and shows in vivo RNA degradation phenotypes similar to those resulting from exosome depletion. In contrast, mutations in Rrp41, the only subunit carrying a conserved phosphorolytic site, appear phenotypically not different from wild-type yeast. We observed that the yeast exosome ring mediates interactions with protein partners, providing an explanation for its essential function.
- Equipe labellisée La Ligue, Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique UPR2167, associée à l'Université Pierre et Marie Curie, Avenue de la Terrasse, 91198 Gif sur Yvette Cedex, France.
- European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
-
Present address: Department of Genetics and Biotechnology, Warsaw University, Pawi
skiego 5a, 02106 Warsaw, Poland. - Max Planck Institute for Biochemistry, AM Klopferspitz, 18, Martinstied D82 152, Germany.
Correspondence to: Bertrand Séraphin1 e-mail: seraphin@cgm.cnrs-gif.fr
Correspondence to: Andrzej Dziembowski1,3 e-mail: andrzejd@ibb.waw.pl
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