The redox‐sensing regulator YodB senses quinones and diamide <i>via</i> a thiol‐disulfide switch in <i>Bacillus subtilis</i>

Khanh, Bui; Albrecht, Dirk; Gronau, Katrin; Becher, Dörte; Hecker, Michael; Antelmann, Haike

doi:10.1002/pmic.201000230

Cited by 35 publications

(55 citation statements)

References 38 publications

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“…Human pathogens such as S. aureus, on the other hand, must develop a certain counteractive defense mechanism to tackle quinone molecules. To study quinone signaling, we focused on S. aureus QsrR (SAV2123), a homolog of B. subtilis quinone stress- sensing regulator YodB (38% identities, 61% positives) (19,21). We first performed a disk-diffusion assay to examine the role of QsrR in response to quinone stress.…”

Section: Resultsmentioning

confidence: 99%

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Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR

Zhang

Jones

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Section: Resultsmentioning

confidence: 99%

“…In Escherichia coli, the anoxic redox control ArcAB is considered a quinone-sensing two-component system (17,18). In Bacillus subtilis, the thiol-stress sensing regulator YodB is a prototypical transcriptional regulator responsible for quinone sensing and detoxification (19)(20)(21).…”

Section: Molecular Mechanism Of Quinone Signaling Mediated Through S-mentioning

confidence: 99%

Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR

Zhang

Jones

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…Immunoprecipitated subunits of RNAP were separated by SDS-PAGE. The ␣ bands were excised and tryptically digested as described previously (53). The resulting peptides were analyzed in a LTQ OrbitrapXL mass spectrometer as described under "Materials and Methods."…”

Section: Tablementioning

confidence: 99%

Inhibition of Acetyl Phosphate-dependent Transcription by an Acetylatable Lysine on RNA Polymerase

Lima

Huyền

Bäsell

et al. 2012

Journal of Biological Chemistry

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“…YodB senses quinones and diamide via the conserved Cys6 residue, which is required for DNA-binding activity and redox sensing of YodB in vivo (15). In recent studies, we have shown that YodB functions as a two-Cys-type redox-sensing regulator that is regulated via intersubunit disulfides between Cys6 and one of the C-terminal Cys residues, Cys101 or Cys108, in response to diamide and quinones in vivo (4). Thus, YodB regulation is similar to that of the two-Cys-type OhrR repressor of Xanthomonas campestris (26).…”

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confidence: 99%

“…However, we also found the glyceraldehyde-3-phosphate dehydrogenase GapA as a target for reversible thiol oxidation by quinones in vivo. Thus, quinones act via the oxidative and electrophilic mode in B. subtilis cells in vivo.The depletion of the thiol redox buffer by diamide and quinones causes a general electrophile stress response in B. subtilis, which includes expression of regulons controlled by the Spx, CtsR, PerR, and CymR regulators and the MarR-type repressors MhqR and YodB (1,4,15,16,21,22,31). YodB is a MarR/DUF24-family repressor that controls the azoreductase AzoR1, the nitroreductase YodC, and the redox-sensing regulator Spx in response to diamide and quinones.…”

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confidence: 99%

The Paralogous MarR/DUF24-Family Repressors YodB and CatR Control Expression of the Catechol Dioxygenase CatE inBacillus subtilis

et al. 2010

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The redox-sensing MarR/DUF24-type repressor YodB controls expression of the azoreductase AzoR1 and the nitroreductase YodC that are involved in detoxification of quinones and diamide in Bacillus subtilis. In the present paper, we identified YodB and its paralog YvaP (CatR) as repressors of the yfiDE (catDE) operon encoding a catechol-2,3-dioxygenase that also contributes to quinone resistance. Inactivation of both CatR and YodB is required for full derepression of catDE transcription. DNA-binding assays and promoter mutagenesis studies showed that CatR protects two inverted repeats with the consensus sequence TTAC-N 5 -GTAA overlapping the ؊35 promoter region (BS1) and the transcriptional start site (TSS) (BS2). The BS1 operator was required for binding of YodB in vitro. CatR and YodB share the conserved N-terminal Cys residue, which is required for redox sensing of CatR in vivo as shown by Cys-to-Ser mutagenesis. Our data suggest that CatR is modified by intermolecular disulfide formation in response to diamide and quinones in vitro and in vivo. Redox regulation of CatR occurs independently of YodB, and no protein interaction was detected between CatR and YodB in vivo using protein cross-linking and mass spectrometry.Bacillus subtilis is exposed in the soil to a variety of antimicrobial agents that include phenolic and quinone-like compounds which are produced by other soil bacteria, plants, or fungi. In addition, quinone-like compounds are present in humic substances of the soil. Quinones are also biologically active compounds that function as lipid electron carriers in the electron transport chain (e.g., ubiquinone and menadione). Thus, quinones are naturally occurring electrophilic compounds that are ubiquitously distributed in bacterial systems.Proteomic and transcriptomic approaches revealed that catechol and methylhydroquinone (MHQ) act like diamide as thiol-reactive electrophiles in B. subtilis. Quinones and diamide deplete the cellular pool of low-molecular-weight (LMW) thiols via different mechanisms. Diamide leads to an increase in reversible thiol modifications, such as inter-and intramolecular disulfides and S thiolations (disulfides between proteins and LMW thiols) (9, 10, 27). Quinones can act as oxidants or electrophiles (13,20,25). As oxidants, quinones redox cycle with their semiquinones, producing reactive oxygen species (ROS), such as superoxide anion or hydrogen peroxide (18). The production of ROS could lead in turn to reversible thiol modifications. As electrophiles, quinones can form S adducts with cellular thiols via the thiol-(S)-alkylation chemistry. Recently, we showed that toxic quinones react mainly via S-alkylation with cellular thiol-containing proteins in vivo, which leads to aggregation and depletion of proteins in the proteome (18). However, we also found the glyceraldehyde-3-phosphate dehydrogenase GapA as a target for reversible thiol oxidation by quinones in vivo. Thus, quinones act via the oxidative and electrophilic mode in B. subtilis cells in vivo.The depletion of the th...

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The redox‐sensing regulator YodB senses quinones and diamide via a thiol‐disulfide switch in Bacillus subtilis

Cited by 35 publications

References 38 publications

Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR

Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR

Inhibition of Acetyl Phosphate-dependent Transcription by an Acetylatable Lysine on RNA Polymerase

The Paralogous MarR/DUF24-Family Repressors YodB and CatR Control Expression of the Catechol Dioxygenase CatE inBacillus subtilis

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