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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216224:14310/15:00080836

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Journal of proteomics

ISSN

1874-3919

e-ISSN

—

Svazek periodika

125

Číslo periodika v rámci svazku

July 01

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

68-75

Kód UT WoS článku

000357243000006

EID výsledku v databázi Scopus

2-s2.0-84939417529