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.

Basic information

Original name

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

Name in Czech

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

Authors

PERNIKÁŘOVÁ, Vendula (203 Czech Republic, belonging to the institution), Vojtěch SEDLÁČEK (203 Czech Republic, belonging to the institution), David POTĚŠIL (203 Czech Republic, belonging to the institution), Iva PROCHÁZKOVÁ (203 Czech Republic, belonging to the institution), Zbyněk ZDRÁHAL (203 Czech Republic, belonging to the institution), Pavel BOUCHAL (203 Czech Republic, belonging to the institution) and Igor KUČERA (203 Czech Republic, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.867

RIV identification code

RIV/00216224:14310/15:00080836

Organization unit

Faculty of Science

DOI

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

UT WoS

000357243000006

Keywords in English

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

Abstract

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.

Links

ED1.1.00/02.0068, research and development project

Name: CEITEC - central european institute of technology

GAP503/12/0369, research and development project

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

Investor: Czech Science Foundation

GA14-19250S, research and development project

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

Investor: Czech Science Foundation

Citovat

PERNIKÁŘOVÁ, Vendula, Vojtěch SEDLÁČEK, David POTĚŠIL, Iva PROCHÁZKOVÁ, Zbyněk ZDRÁHAL, Pavel BOUCHAL and 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, vol. 125, July, p. 68-75. ISSN 1874-3919. Available from: 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 and 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, vol.~125, July, p.~68-75. ISSN~1874-3919. Available from: https://dx.doi.org/10.1016/j.jprot.2015.05.002.

Detailed Information on Publication Record