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J. Biol. Chem., Vol. 283, Issue 21, 14366-14375, May 23, 2008

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Biochemical and Structural Insights into Bacterial Organelle Form and Biogenesis^*

Joshua B. Parsons¹, Sriramulu D. Dinesh¹, Evelyne Deery, Helen K. Leech, Amanda A. Brindley, Dana Heldt, Steffanie Frank, C. Mark Smales, Heinrich Lünsdorf^¶, Alain Rambach^||, Mhairi H. Gass^**, Andrew Bleloch^**, Kirsty J. McClean, Andrew W. Munro, Stephen E. J. Rigby, Martin J. Warren², and Michael B. Prentice³

From the Protein Science Group, Department of Biochemistry, University of Kent, Canterbury, Kent CT2 7NJ, United Kingdom, Departments of Pathology and Microbiology, University College Cork, Cork, Ireland, ^¶Department of Vaccinology, Helmholtz Center of Infection Research, Braunschweig D-38124, Germany, ^||CHROMagar, 4 place du 18 Juin 1940, F-75006 Paris, France, ^**SuperSTEM Facility, Daresbury Laboratories, Daresbury WA4 4AD, United Kingdom, Faculty of Life Sciences, Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom, and School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, United Kingdom

Many heterotrophic bacteria have the ability to make polyhedral structures containing metabolic enzymes that are bounded by a unilamellar protein shell (metabolosomes or enterosomes). These bacterial organelles contain enzymes associated with a specific metabolic process (e.g. 1,2-propanediol or ethanolamine utilization). We show that the 21 gene regulon specifying the pdu organelle and propanediol utilization enzymes from Citrobacter freundii is fully functional when cloned in Escherichia coli, both producing metabolosomes and allowing propanediol utilization. Genetic manipulation of the level of specific shell proteins resulted in the formation of aberrantly shaped metabolosomes, providing evidence for their involvement as delimiting entities in the organelle. This is the first demonstration of complete recombinant metabolosome activity transferred in a single step and supports phylogenetic evidence that the pdu genes are readily horizontally transmissible. One of the predicted shell proteins (PduT) was found to have a novel Fe-S center formed between four protein subunits. The recombinant model will facilitate future experiments establishing the structure and assembly of these multiprotein assemblages and their fate when the specific metabolic function is no longer required.

Received for publication, November 9, 2007 , and in revised form, March 10, 2008.

^* This work was supported by the Science Foundation Ireland (Research Frontiers Programme 05-RF-GEN053) and the Biotechnology and Biological Sciences Research Council. 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 Figs. S1–S3 and Tables S1 and S2.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AM498294.

¹ These authors contributed equally to this work.

² To whom correspondence may be addressed. Tel.: 44-1227-824690; E-mail: m.j.warren{at}kent.ac.uk. ³ To whom correspondence may be addressed. Tel.: 353-21-4901420; E-mail: m.prentice{at}ucc.ie.

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