Proteomics of the organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans adapted to tetrachloroethene and other energy substrates

Organohalide respiration is an environmentally important but poorly characterized type of anaerobic respiration. We compared the global proteome of the versatile organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans grown with different electron acceptors (fumarate, nitrate, or...

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Bibliographic Details
Published in:Scientific reports 2015-09, Vol.5 (1), p.13794-13794, Article 13794
Main Authors: Goris, Tobias, Schiffmann, Christian L, Gadkari, Jennifer, Schubert, Torsten, Seifert, Jana, Jehmlich, Nico, von Bergen, Martin, Diekert, Gabriele
Format: Article
Language:English
Subjects:
Anaerobic respiration
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Dehydrogenases
Energy Metabolism - genetics
Energy Metabolism - physiology
Energy resources
Epsilonproteobacteria - genetics
Epsilonproteobacteria - metabolism
Ferredoxin
Ferredoxins - metabolism
Formates - metabolism
Gene Expression Profiling
Hydroquinone
Nitrates
Nitrates - metabolism
Oxidoreductases - genetics
Oxidoreductases - metabolism
Oxygen Consumption
Peroxidase
Principal Component Analysis
Proteins
Proteomics
Pyruvic acid
Pyruvic Acid - metabolism
Quinones
Quinones - metabolism
Respiration
Tetrachloroethylene - metabolism
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Summary:Organohalide respiration is an environmentally important but poorly characterized type of anaerobic respiration. We compared the global proteome of the versatile organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans grown with different electron acceptors (fumarate, nitrate, or tetrachloroethene [PCE]). The most significant differences in protein abundance were found for gene products of the organohalide respiration region. This genomic region encodes the corrinoid and FeS cluster containing PCE reductive dehalogenase PceA and other proteins putatively involved in PCE metabolism such as those involved in corrinoid biosynthesis. The latter gene products as well as PceA and a putative quinol dehydrogenase were almost exclusively detected in cells grown with PCE. This finding suggests an electron flow from the electron donor such as formate or pyruvate via the quinone pool and a quinol dehydrogenase to PceA and the terminal electron acceptor PCE. Two putative accessory proteins, an IscU-like protein and a peroxidase-like protein, were detected with PCE only and might be involved in PceA maturation. The proteome of cells grown with pyruvate instead of formate as electron donor indicates a route of electrons from reduced ferredoxin via an Epsilonproteobacterial complex I and the quinone pool to PCE.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep13794