Proteomics

Dataset Information

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Proteomic analysis of Shewanella oneidensis overexpressing or not the putrescin decarboxylase speC


ABSTRACT: Some microorganisms can respire with extracellular electron acceptors using an extended electron transport chain to the cell surface. These organisms apply flavin molecules as cofactors to facilitate one-electron transfer catalysed by the terminal reductases and as endogenous electron shuttles. In the model organism Shewanella oneidensis, riboflavin production and excretion triggers a specific biofilm formation response that is initiated at a specific threshold concentration, similar to canonical quorum sensing molecules. Riboflavin-mediated messaging is based on the overexpression of the gene encoding the putrescin decarboxylase speC which leads to posttranscriptional overproduction of proteins involved in biofilm formation. We performed a mass spectrometry-based analysis of cells with and without speC overexpression to identify the effect of SpeC overexpression on the cell proteome.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Shewanella Oneidensis (strain Mr-1)

SUBMITTER: Yohann Couté  

LAB HEAD: Virginie Brun

PROVIDER: PXD025681 | Pride | 2021-07-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Mut-1.mgf Mgf
Mut-1.raw Raw
Mut-2.mgf Mgf
Mut-2.raw Raw
Mut-3.mgf Mgf
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Publications

Extracellular riboflavin induces anaerobic biofilm formation in Shewanella oneidensis.

Edel Miriam M   Sturm Gunnar G   Sturm-Richter Katrin K   Wagner Michael M   Ducassou Julia Novion JN   Couté Yohann Y   Horn Harald H   Gescher Johannes J  

Biotechnology for biofuels 20210603 1


<h4>Background</h4>Some microorganisms can respire with extracellular electron acceptors using an extended electron transport chain to the cell surface. This process can be applied in bioelectrochemical systems in which the organisms produce an electrical current by respiring with an anode as electron acceptor. These organisms apply flavin molecules as cofactors to facilitate one-electron transfer catalyzed by the terminal reductases and in some cases as endogenous electron shuttles.<h4>Results<  ...[more]

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