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Originally published In Press as doi:10.1074/jbc.M512495200 on December 28, 2005

J. Biol. Chem., Vol. 281, Issue 10, 6751-6759, March 10, 2006
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The Pyrococcus Exosome Complex

STRUCTURAL AND FUNCTIONAL CHARACTERIZATION*Formula

Celso Raul Romero Ramos{ddagger}1, Cristiano L. P. Oliveira§2, Iris L. Torriani§, and Carla Columbano Oliveira{ddagger}3

From the {ddagger}Department of Biochemistry, Chemistry Institute, University of São Paulo, 05508-900 São Paulo, SP, Brazil, §Brazilian Synchrotron Light Laboratory, 13084-971 Campinas, SP, Brazil, and Physics Institute, State University of Campinas, 13084-971 Campinas, SP, Brazil

The exosome is a conserved eukaryotic enzymatic complex that plays an essential role in many pathways of RNA processing and degradation. Here, we describe the structural characterization of the predicted archaeal exosome in solution using small angle x-ray scattering. The structure model calculated from the small angle x-ray scattering pattern provides an indication of the existence of a disk-shaped structure, corresponding to the "RNases PH ring" complex formed by the proteins aRrp41 and aRrp42. The RNases PH ring complex corresponds to the core of the exosome, binds RNA, and has phosphorolytic and polymerization activities. Three additional molecules of the RNA-binding protein aRrp4 are attached to the core as extended and flexible arms that may direct the substrates to the active sites of the exosome. In the presence of aRrp4, the activity of the core complex is enhanced, suggesting a regulatory role for this protein. The results shown here also indicate the participation of the exosome in RNA metabolism in Archaea, as was established in Eukarya.


Received for publication, November 22, 2005 , and in revised form, December 19, 2005.

* This work was supported by Fundação de Amparo à Pesquisa do Estado de São Paulo SMOLBnet Grant 01/07543-2 and by Laboratório Nacional de Luz Síncrotron under project 1436 (proposals 3447 and 4087). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Formula The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. 1 and 2.

1 Recipient of Fundação de Amparo à Pesquisa do Estado de São Paulo fellowship 02/00207.

2 Recipient of Fundação de Amparo à Pesquisa do Estado de São Paulo fellowship 00/15087-4 and of a Conselho Nacional de Desenvolvimento Cientifico e Tecnológico fellowship (381600/2005-0).

3 To whom correspondence should be addressed: Dept. of Biochemistry, Chemistry Institute, University of São Paulo, Av. Prof. Lineu Prestes 748, CEP 05508-900, São Paulo, SP, Brazil. Tel.: 55-11-30913810 (ext. 208); Fax: 55-11-38155579; E-mail ccoliv{at}iq.usp.br.


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