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

J 2015

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

PERNIKÁŘOVÁ, Vendula, Vojtěch SEDLÁČEK, David POTĚŠIL, Iva PROCHÁZKOVÁ, Zbyněk ZDRÁHAL et. al.

Základní údaje

Originální název

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

Název česky

Proteomická odezva na oxidační stres vyvolaný methylviologenem u divokého a FerB-mutentního kmene Paracoccus denitrificans

Autoři

PERNIKÁŘOVÁ, Vendula (203 Česká republika, domácí), Vojtěch SEDLÁČEK (203 Česká republika, domácí), David POTĚŠIL (203 Česká republika, domácí), Iva PROCHÁZKOVÁ (203 Česká republika, domácí), Zbyněk ZDRÁHAL (203 Česká republika, domácí), Pavel BOUCHAL (203 Česká republika, domácí) a Igor KUČERA (203 Česká republika, garant, domácí)

Vydání

Journal of Proteomics, Amsterdam, ELSEVIER SCIENCE BV, 2015, 1874-3919

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.867

Kód RIV

RIV/00216224:14310/15:00080836

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1016/j.jprot.2015.05.002

UT WoS

000357243000006

Klíčová slova anglicky

Paracoccus denitrificans; methyl viologen; oxidative stress; flavoprotein; flavin reductase; microbial proteomics

Štítky

AKR, CF PROT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 20. 7. 2019 14:21, prof. RNDr. Igor Kučera, DrSc.

Anotace

V originále

FerB is a cytoplasmic flavoprotein from the soil bacterium Paracoccus denitrificans with a putative role in defense against oxidative stress. To further explore this hypothesis, we compared protein variations upon methyl viologen treatment in wild-type and FerB mutant strains by a quantitative proteomic analysis based on iTRAQ-3DLC–MS/MS analysis. The proteins showing the most prominent increase in abundance were 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 down-regulation 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. While the level of FerB remained relatively constant, two proteins homologous to FerB accumulated during oxidative stress. When their genes were expressed in Escherichia coli, neither of the protein products contained a bound flavin, whereas they both had a high activity of flavin reductase, one preferentially utilizing NADH and the other NADPH.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP503/12/0369, projekt VaV

Název: Nové flavin-dependentní enzymy Paracoccus denitrificans: reakční mechanismy, metabolické funkce a úloha v buněčném oxidačním stresu

Investor: Grantová agentura ČR, Nové flavin-dependentní enzymy Paracoccus denitrificans: reakční mechanismy, metabolické funkce a úloha v buněčném oxidačním stresu

GA14-19250S, projekt VaV

Název: Nový panel proteinů korelujících se stavem lymfatických uzlin u low-grade nádorů prsu: Klinická verifikace a úloha v invazivitě nádorových buněk

Investor: Grantová agentura ČR, Nový panel proteinů korelujících se stavem lymfatických uzlin u low-grade nádorů prsu: Klinická verifikace a úloha v invazivitě nádorových buněk

Citovat

PERNIKÁŘOVÁ, Vendula, Vojtěch SEDLÁČEK, David POTĚŠIL, Iva PROCHÁZKOVÁ, Zbyněk ZDRÁHAL, Pavel BOUCHAL a Igor KUČERA. Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans. Journal of Proteomics. Amsterdam: ELSEVIER SCIENCE BV, 2015, roč. 125, July, s. 68-75. ISSN 1874-3919. Dostupné z: https://dx.doi.org/10.1016/j.jprot.2015.05.002.

@article{1300690,
   author = {Pernikářová, Vendula and Sedláček, Vojtěch and Potěšil, David and Procházková, Iva and Zdráhal, Zbyněk and Bouchal, Pavel and Kučera, Igor},
   article_location = {Amsterdam},
   article_number = {July},
   doi = {http://dx.doi.org/10.1016/j.jprot.2015.05.002},
   keywords = {Paracoccus denitrificans; methyl viologen; oxidative stress; flavoprotein; flavin reductase; microbial proteomics},
   language = {eng},
   issn = {1874-3919},
   journal = {Journal of Proteomics},
   title = {Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans},
   url = {http://www.sciencedirect.com/science/article/pii/S1874391915002201},
   volume = {125},
   year = {2015}
}

TY  - JOUR
ID  - 1300690
AU  - Pernikářová, Vendula - Sedláček, Vojtěch - Potěšil, David - Procházková, Iva - Zdráhal, Zbyněk - Bouchal, Pavel - Kučera, Igor
PY  - 2015
TI  - Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans
JF  - Journal of Proteomics
VL  - 125
IS  - July
SP  - 68-75
EP  - 68-75
PB  - ELSEVIER SCIENCE BV
SN  - 18743919
KW  - Paracoccus denitrificans
KW  - methyl viologen
KW  - oxidative stress
KW  - flavoprotein
KW  - flavin reductase
KW  - microbial proteomics
UR  - http://www.sciencedirect.com/science/article/pii/S1874391915002201
L2  - http://www.sciencedirect.com/science/article/pii/S1874391915002201
N2  - FerB is a cytoplasmic flavoprotein from the soil bacterium Paracoccus denitrificans with a putative role in defense against oxidative stress. To further explore this hypothesis, we compared protein variations upon methyl viologen treatment in wild-type and FerB mutant strains by a quantitative proteomic analysis based on iTRAQ-3DLC–MS/MS analysis. The proteins showing the most prominent increase in abundance were 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 down-regulation 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. While the level of FerB remained relatively constant, two proteins homologous to FerB accumulated during oxidative stress. When their genes were expressed in Escherichia coli, neither of the protein products contained a bound flavin, whereas they both had a high activity of flavin reductase, one preferentially utilizing NADH and the other NADPH.
ER  -

PERNIKÁŘOVÁ, Vendula, Vojtěch SEDLÁČEK, David POTĚŠIL, Iva PROCHÁZKOVÁ, Zbyněk ZDRÁHAL, Pavel BOUCHAL a Igor KUČERA. Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans. \textit{Journal of Proteomics}. Amsterdam: ELSEVIER SCIENCE BV, 2015, roč.~125, July, s.~68-75. ISSN~1874-3919. Dostupné z: https://dx.doi.org/10.1016/j.jprot.2015.05.002.

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