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Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F15%3A%230000620" target="_blank" >RIV/00209805:_____/15:#0000620 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/15:00080836

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.jprot.2015.05.002" target="_blank" >http://dx.doi.org/10.1016/j.jprot.2015.05.002</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.jprot.2015.05.002" target="_blank" >10.1016/j.jprot.2015.05.002</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans

  • Original language description

    FerB is a cytoplasmic flavoprotein fromthe soil bacteriumParacoccus denitrificanswith a putative role in defense against oxidative stress. To further explore this hypothesis, we compared protein variations upon methyl viologen treatment in wild-type andFerB mutant strains by a quantitative proteomic analysis based on iTRAQ- 3DLC?MS/MS analysis. The proteins showing themost prominent increase in abundancewere assigned to carbon fixation and sulfur assimilatory pathways. By employing these proteins as indirect markers, oxidative stress was found to be 15% less severe in the wild-type than in the FerB-deficient mutant cells. Oxidative stress altered the levels of proteins whose expression is dependent on the transcriptional factor FnrP. The observed downregulation of the fnrP regulon members, most notably that of nitrous oxide reductase, was tentatively explained by an oxidative degradation of the [4Fe?4S] center of FnrP leading to a protein form which no longer activates transcription.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of proteomics

  • ISSN

    1874-3919

  • e-ISSN

  • Volume of the periodical

    125

  • Issue of the periodical within the volume

    July 01

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    8

  • Pages from-to

    68-75

  • UT code for WoS article

    000357243000006

  • EID of the result in the Scopus database

    2-s2.0-84939417529