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
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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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
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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