EMBO reports
EMBO reports
SEARCH Go
My AccountSubmit manuscriptSubscribeRegisterHelp
Journal home
Press releases
Aims and scope
Authors and referees
 Guide for authors
 Guide for referees
 Contact editors
 Advisors & Advisory
 Editorial Board
 Submit a Manuscript
Customer Services
 Subscriptions
 Order sample copy
 Purchase articles
 Reprints and
  permissions
 Contact NPG
 Advertising
EMBO
EMBO
www.embo.org

scientific report
EMBO reports 8, 5, 470–476 (2007)
doi:10.1038/sj.embor.7400945
AOP Published online: 23 March 2007

RNA channelling by the archaeal exosome

Esben Lorentzen1, 2, Andrzej Dziembowski3, Doris Lindner1, Bertrand Seraphin3 & Elena Conti1, 2
1 European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, D-69117, Heidelberg, Germany
2 Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152, Martinsried, Germany
3 Equipe Labellisée La Ligue, CGM, CNRS UPR2167, Associée à l'Université Pierre et Marie Curie, Avenue de la Terrasse, 91198 Gif sur Yvette Cedex, France


To whom correspondence should be addressed

Esben Lorentzen Tel: +49 6221 3878537; Fax: +49 6221 387 8519; E-mail: lorentze@embl.de
Elena Conti Tel: +49 6221 3878537; Fax: +49 6221 387 8519; E-mail: conti@embl.de


 Present address: Department of Genetics & Biotechnology, Warsaw University, Pawinskiego 5a, Poland

Received 6 December 2006; Accepted 5 February 2007; Published online 23 March 2007.
Abstract

Exosomes are complexes containing 3' right arrow 5' exoribonucleases that have important roles in processing, decay and quality control of various RNA molecules. Archaeal exosomes consist of a hexameric core of three active RNase PH subunits (ribosomal RNA processing factor (Rrp)41) and three inactive RNase PH subunits (Rrp42). A trimeric ring of subunits with putative RNA-binding domains (Rrp4/cep1 synthetic lethality (Csl)4) is positioned on top of the hexamer on the opposite side to the RNA degrading sites. Here, we present the 1.6 Å resolution crystal structure of the nine-subunit exosome of Sulfolobus solfataricus and the 2.3 Å structure of this complex bound to an RNA substrate designed to be partly trimmed rather than completely degraded. The RNA binds both at the active site on one side of the molecule and on the opposite side in the narrowest constriction of the central channel. Multiple substrate-binding sites and the entrapment of the substrate in the central channel provide a rationale for the processive degradation of extended RNAs and the stalling of structured RNAs.

Top

MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated

NEWS AND VIEWS

Threaded for degradation

Nature Structural & Molecular Biology News and Views (01 Dec 2005)

Wrong PH for RNA degradation

Nature Structural & Molecular Biology News and Views (01 Jan 2007)

Doughnuts dealing with RNA

Nature Structural & Molecular Biology News and Views (01 Jul 2005)

RNase II structure completes group portrait of 3′ exoribonucleases

Nature Structural & Molecular Biology News and Views (01 Sep 2006)

top go to top
This article

Email
Email link to a friend
Download PDF Download PDF
 Full TextFull text
 rights and permissions Rights and permissions
 order commercial reprints Reprints
Privacy PolicyCopyright © 2007 by the European Molecular Biology Organization