Comparative proteomics implicates a role for multiple secretion systems in electrode-respiring Geobacter sulfurreducens biofilms
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Geobacter sulfurreducens is a dissimilatory metal-reducing bacterium capable of forming thick electron-conducting biofilms on solid electrodes. Here, we employ for the first time comparative proteomics to identify key physiological changes involved in G. sulfurreducens adaptation from fumarate-respiring planktonic cells to electron-conducting biofilms. Increased levels of proteins involved in outer membrane biogenesis, cell motility and secretion are expressed in biofilms. Of particular importance to the electron-conducting biofilms are proteins associated with secretion systems of Type I, II, V and Type IV pili. Furthermore, enzymes involved in lipopolysaccharide and peptidoglycan biosynthesis show increased levels of expression in electron-conducting biofilms compared to planktonic cells. These observations point to similarities in long-range electron transfer mechanisms between G. sulfurreducens and Shewanella oneidensis, while highlighting the wider significance of secretion systems beyond that of Type IV pili identified to date in the adaptation of G. sulfurreducens to electrode respiration.
Kavanagh , P , Botting , C H , Jana , P S , Leech , D & Abram , F 2016 , ' Comparative proteomics implicates a role for multiple secretion systems in electrode-respiring Geobacter sulfurreducens biofilms ' Journal of Proteome Research , vol 15 , no. 12 , pp. 4135-4145 . DOI: 10.1021/acs.jproteome.5b01019
Journal of Proteome Research
Copyright © 2016 American Chemical Society. This work has been made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at: https://doi.org/10.1021/acs.jproteome.5b01019
DescriptionThis work was supported by Science Foundation Ireland (Charles Parsons Energy Research Award - 06/CP/E006) and the Wellcome Trust (grant number 094476/Z/10/Z) which funded the purchase of the TripleTOF 5600 mass spectrometer at the BSRC Mass Spectrometry and Proteomics Facility, University of St Andrews. The authors thank Matthew A. Fuszard and Sally L. Shirran for their technical assistance with fractionation and mass spectrometry.
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