Details
| Original language | English |
|---|---|
| Pages (from-to) | 777-784 |
| Number of pages | 8 |
| Journal | Biological chemistry |
| Volume | 391 |
| Issue number | 7 |
| Publication status | Published - 1 Jul 2010 |
Abstract
The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The in vivo effects of the lack of RhdA were investigated using an A. vinelandii mutant strain (MV474) in which the rhdA gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the rhdA gene generates an oxidative stress condition to which A. vinelandii responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of rhdA gene expression was observed, thus highlighting that RhdA is important for A. vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed.
Keywords
- oxidative stress, transcriptomic analyses
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
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In: Biological chemistry, Vol. 391, No. 7, 01.07.2010, p. 777-784.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The rhodanese RhdA helps azotobacter vinelandii in maintaining cellular redox balance
AU - Remelli, William
AU - Cereda, Angelo
AU - Papenbrock, Jutta
AU - Forlani, Fabio
AU - Pagani, Silvia
N1 - Funding information: Mobility of researchers between Italy and Germany was sponsored by Vigoni project n. 0815171 (2009–2010; Ateneo Italo-Tedesco, Deutscher Akademischer Austauschdienst) to F.F. and J.P. We thank Dr. Aristodemo Carpen for skilful technical assistance.
PY - 2010/7/1
Y1 - 2010/7/1
N2 - The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The in vivo effects of the lack of RhdA were investigated using an A. vinelandii mutant strain (MV474) in which the rhdA gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the rhdA gene generates an oxidative stress condition to which A. vinelandii responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of rhdA gene expression was observed, thus highlighting that RhdA is important for A. vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed.
AB - The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The in vivo effects of the lack of RhdA were investigated using an A. vinelandii mutant strain (MV474) in which the rhdA gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the rhdA gene generates an oxidative stress condition to which A. vinelandii responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of rhdA gene expression was observed, thus highlighting that RhdA is important for A. vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed.
KW - oxidative stress
KW - transcriptomic analyses
UR - http://www.scopus.com/inward/record.url?scp=77954584840&partnerID=8YFLogxK
U2 - 10.1515/BC.2010.073
DO - 10.1515/BC.2010.073
M3 - Article
C2 - 20482308
AN - SCOPUS:77954584840
VL - 391
SP - 777
EP - 784
JO - Biological chemistry
JF - Biological chemistry
SN - 1431-6730
IS - 7
ER -