-
Something wrong with this record ?
Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans
V. Pernikářová, V. Sedláček, D. Potěšil, I. Procházková, Z. Zdráhal, P. Bouchal, I. Kučera,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Bacterial Proteins biosynthesis genetics MeSH
- Flavoproteins genetics metabolism MeSH
- Mutation * MeSH
- Oxidative Stress drug effects genetics MeSH
- Paracoccus denitrificans genetics metabolism MeSH
- Paraquat pharmacology MeSH
- Proteomics MeSH
- Gene Expression Regulation, Bacterial drug effects genetics MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc16010192
- 003
- CZ-PrNML
- 005
- 20190204100133.0
- 007
- ta
- 008
- 160408s2015 ne f 000 0|engg|
- 009
- AR
- 024 7_
- $a 10.1016/j.jprot.2015.05.002 $2 doi
- 035 __
- $a (PubMed)25976748
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a ne
- 100 1_
- $a Pernikářová, Vendula $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic.
- 245 10
- $a Proteomic responses to a methyl viologen-induced oxidative stress in the wild type and FerB mutant strains of Paracoccus denitrificans / $c V. Pernikářová, V. Sedláček, D. Potěšil, I. Procházková, Z. Zdráhal, P. Bouchal, I. Kučera,
- 520 9_
- $a 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.
- 650 _2
- $a bakteriální proteiny $x biosyntéza $x genetika $7 D001426
- 650 _2
- $a flavoproteiny $x genetika $x metabolismus $7 D005420
- 650 _2
- $a regulace genové exprese u bakterií $x účinky léků $x genetika $7 D015964
- 650 12
- $a mutace $7 D009154
- 650 _2
- $a oxidační stres $x účinky léků $x genetika $7 D018384
- 650 _2
- $a Paracoccus denitrificans $x genetika $x metabolismus $7 D010231
- 650 _2
- $a paraquat $x farmakologie $7 D010269
- 650 _2
- $a proteomika $7 D040901
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Sedláček, Vojtěch $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic.
- 700 1_
- $a Potěšil, David $u Central European Institute for Technology, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic.
- 700 1_
- $a Procházková, Iva $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic; Regional Centre for Applied Molecular Oncology, Masaryk Memorial Cancer Institute, Žlutý kopec 7, 65653 Brno, Czech Republic.
- 700 1_
- $a Zdráhal, Zbyněk $u Central European Institute for Technology, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic.
- 700 1_
- $a Bouchal, Pavel, $7 xx0128495 $d 1975- $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic. Electronic address: bouchal@chemi.muni.cz.
- 700 1_
- $a Kučera, Igor $u Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic. Electronic address: ikucera@chemi.muni.cz.
- 773 0_
- $w MED00166847 $t Journal of proteomics $x 1876-7737 $g Roč. 125, č. - (2015), s. 68-75
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/25976748 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20160408 $b ABA008
- 991 __
- $a 20190204100410 $b ABA008
- 999 __
- $a ok $b bmc $g 1113621 $s 934560
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2015 $b 125 $c - $d 68-75 $e 20150511 $i 1876-7737 $m Journal of proteomics $n J Proteomics $x MED00166847
- LZP __
- $a Pubmed-20160408
