Parsons, J.B. and Dinesh, S.D. and Deery, E. and Leech, H.K. and Brindley, A.A. and Heldt, D. and Frank, S. and Smales, C.M. and Lunsdorf, H. and Rambach, A. and Gass, M.H. and Bleloch, A. and McClean, K.J. and Munro, A.W. and Rigby, S.E. and Warren, M.J. and Prentice, M.B. (2008) Biochemical and Structural Insights into Bacterial Organelle Form and Biogenesis. Journal of Biochemistry, 283 (21). pp. 14366-14375. ISSN 0021-9258 (Print).
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Abstract
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.
| Item Type: | Article |
|---|---|
| Subjects: | Q Science |
| Divisions: | Faculties > Science Technology and Medical Studies > School of Biosciences |
| Depositing User: | Mark Smales |
| Date Deposited: | 13 Mar 2009 10:22 |
| Last Modified: | 14 Jan 2010 14:23 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/6236 (The current URI for this page, for reference purposes) |
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