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J. Biol. Chem., Vol. 282, Issue 3, 1882-1890, January 19, 2007

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Functional and Phylogenetic Properties of the Pore-forming -Barrel Transporters of the Omp85 Family^*

Rolf Bredemeier¹, Thomas Schlegel¹², Franziska Ertel³, Aleksandar Vojta, Ljudmila Borissenko^¶, Markus T. Bohnsack^||4, Michael Groll^¶, Arndt von Haeseler^**, and Enrico Schleiff⁵

From the Ludwig Maximilians University (LMU), Department of Biology I, Menzinger Strasse 67, 80638 München, Germany, Institut für Informatik, Heinrich-Heine Universität Düsseldorf, D-40225 Düsseldorf, Germany, ^¶LMU, Adolf-Butenandt-Institut für Physiologische Chemie, 81377 München, Germany, ^||Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom, and ^**Center for Integrative Bioinformatics Vienna, Max F. Perutz Laboratories, University of Vienna, Medical University of Vienna, and Veterinary University of Vienna, 1030 Vienna, Austria

-Barrel-shaped channels of the Omp85 family are involved in the translocation or assembly of proteins of bacterial, mitochondrial, and plastidic outer membranes. We have compared these proteins to understand the evolutionary development of the translocators. We have demonstrated that the proteins from proteobacteria and mitochondria have a pore diameter that is at least five times smaller than found for the Omp85 in cyanobacteria and plastids. This finding can explain why Omp85 from cyanobacteria (but not the homologous protein from proteobacteria) was remodeled to become the protein translocation pore after endosymbiosis. Further, the pore-forming region of the Omp85 proteins is restricted to the C terminus. Based on a phylogenetic analysis we have shown that the pore-forming domain displays a different evolutionary relationship than the N-terminal domain. In line with this, the affinity of the N-terminal domain to the C-terminal region of the Omp85 from plastids and cyanobacteria differs, even though the N-terminal domain is involved in gating of the pore in both groups. We have further shown that the N-terminal domain of nOmp85 takes part in homo-oligomerization. Thereby, the differences in the phylogeny of the two domains are explained by different functional constraints acting on the regions. The pore-forming domain, however, is further divided into two functional regions, where the distal C terminus itself forms a dimeric pore. Based on functional and phylogenetic analysis, we suggest an evolutionary scenario that explains the origin of the contemporary translocon.

Received for publication, October 11, 2006 , and in revised form, November 3, 2006.

^* This work was supported in part by the Deutsche Forschungsgemeinschaft (SFBTR1-C7), Fonds der Chemischen Industrie, and Volkswagenstiftung (to E. S.) and from the Wiener Wissenschafts-, Forschungs-, und Technologie-fonds (to A. v. H.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table 1 and Fig. 1.

¹ These authors contributed equally to this work.

² Supported in part by the Düsseldorf-Entrepreneur-Foundation.

³ Current address: LMU, Adolf Butenandt Institute, Molecular Biology, 80336 München, Germany.

⁴ Supported by a Federation of European Biochemical Societies long term fellowship.

⁵ To whom correspondence should be addressed: LMU, VW-Research Group, Menzinger Str. 67, 80638 München, Germany. Tel.: 49-89-17861-182; Fax: 49-89-17861-185; E-mail: schleiff{at}lrz.uni-muenchen.de.

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