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Volumn 14, Issue 6, 2011, Pages 1049-1063

Thiol-based redox switches and gene regulation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DIAMIDE; ELECTROPHILE; HYDROPEROXIDE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; NITRIC OXIDE; PEROXYNITRITE; PROTEIN HISTIDINE KINASE; QUINONE DERIVATIVE; REACTIVE ELECTROPHILIC SPECIES; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; S NITROSOTHIOL; SIGMA FACTOR; THIOL; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR CPRK; TRANSCRIPTION FACTOR CRTJ; TRANSCRIPTION FACTOR NRF2; TRANSCRIPTION FACTOR OHRR; TRANSCRIPTION FACTOR OXYR; TRANSCRIPTION FACTOR REGB; TRANSCRIPTION FACTOR RSRA; TRANSCRIPTION FACTOR SPX; TRANSCRIPTION FACTOR YODB; UNCLASSIFIED DRUG;

EID: 79951906200     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2010.3400     Document Type: Review
Times cited : (314)

References (96)
  • 1
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A, Varghese S, and Imlay JA. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol Microbiol 72: 844-858, 2009.
    • (2009) Mol Microbiol , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 2
    • 39649108459 scopus 로고    scopus 로고
    • Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis
    • DOI 10.1586/14789450.5.1.77
    • Antelmann H, Hecker M, and Zuber P. Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis. Expert Rev Proteom 5: 77-90, 2008. (Pubitemid 351287743)
    • (2008) Expert Review of Proteomics , vol.5 , Issue.1 , pp. 77-90
    • Antelmann, H.1    Hecker, M.2    Zuber, P.3
  • 3
    • 0346996698 scopus 로고    scopus 로고
    • Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: Zinc release and disulfide bond formation
    • Bae JB, Park JH, Hahn MY, Kim MS, and Roe JH. Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: zinc release and disulfide bond formation. J Mol Biol 335: 425-435, 2004.
    • (2004) J Mol Biol , vol.335 , pp. 425-435
    • Bae, J.B.1    Park, J.H.2    Hahn, M.Y.3    Kim, M.S.4    Roe, J.H.5
  • 4
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • DOI 10.1016/j.sbi.2004.09.012, PII S0959440X04001769
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr Opin Struct Biol 14: 679-686, 2004. (Pubitemid 39592578)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.6 , pp. 679-686
    • Barford, D.1
  • 5
    • 64549097266 scopus 로고    scopus 로고
    • Thiol-based redox switches in eukaryotic proteins
    • Brandes N, Schmitt S, and Jakob U. Thiol-based redox switches in eukaryotic proteins. Antioxid Redox Signal 11: 997-1014, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 997-1014
    • Brandes, N.1    Schmitt, S.2    Jakob, U.3
  • 6
    • 0036047672 scopus 로고    scopus 로고
    • Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues
    • DOI 10.1046/j.1365-2958.2002.03020.x
    • Castillo EA, Ayte J, Chiva C, Moldon A, Carrascal M, Abian J, Jones N, and Hidalgo E. Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues. Mol Microbiol 45: 243-254, 2002. (Pubitemid 35025948)
    • (2002) Molecular Microbiology , vol.45 , Issue.1 , pp. 243-254
    • Castillo, E.A.1    Ayte, J.2    Chiva, C.3    Moldon, A.4    Carrascal, M.5    Abian, J.6    Jones, N.7    Hidalgo, E.8
  • 7
    • 45449113598 scopus 로고    scopus 로고
    • A novel OxyR sensor and regulator of hydrogen peroxide stress with one cysteine residue in Deinococcus radiodurans
    • Chen H, Xu G, Zhao Y, Tian B, Lu H, Yu X, Xu Z, Ying N, Hu S, and Hua Y. A novel OxyR sensor and regulator of hydrogen peroxide stress with one cysteine residue in Deinococcus radiodurans. PLoS One 3: e1602, 2008.
    • (2008) PLoS One , vol.3
    • Chen, H.1    Xu, G.2    Zhao, Y.3    Tian, B.4    Lu, H.5    Yu, X.6    Xu, Z.7    Ying, N.8    Hu, S.9    Hua, Y.10
  • 8
    • 77956131582 scopus 로고    scopus 로고
    • The redox-sensing regulator YodB senses quinones and diamide via a thiol-disulfide switch in Bacillus subtilis
    • Chi BK, Albrecht D, Gronau K, Becher D, Hecker M, and Antelmann H. The redox-sensing regulator YodB senses quinones and diamide via a thiol-disulfide switch in Bacillus subtilis. Proteomics 10: 3155-3164, 2010.
    • (2010) Proteomics , vol.10 , pp. 3155-3164
    • Chi, B.K.1    Albrecht, D.2    Gronau, K.3    Becher, D.4    Hecker, M.5    Antelmann, H.6
  • 9
    • 1642394747 scopus 로고    scopus 로고
    • Redox property and regulation of PpsR, a transcriptional repressor of photosystem gene expression in Rhodobacter sphaeroides
    • Cho SH, Youn SH, Lee SR, Yim HS, and Kang SO. Redox property and regulation of PpsR, a transcriptional repressor of photosystem gene expression in Rhodobacter sphaeroides. Microbiology 150: 697-706, 2004.
    • (2004) Microbiology , vol.150 , pp. 697-706
    • Cho, S.H.1    Youn, S.H.2    Lee, S.R.3    Yim, H.S.4    Kang, S.O.5
  • 10
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • DOI 10.1016/S0092-8674(01)00300-2
    • Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, and Ryu SE. Structural basis of the redox switch in the OxyR transcription factor. Cell 105: 103-113, 2001. (Pubitemid 32323920)
    • (2001) Cell , vol.105 , Issue.1 , pp. 103-113
    • Choi, H.-J.1    Kim, S.-J.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.-R.5    Storz, G.6    Ryu, S.-E.7
  • 11
    • 26944499456 scopus 로고    scopus 로고
    • A non-haem iron centre in the transcription factor NorR senses nitric oxide
    • DOI 10.1038/nature03953, PII N03953
    • D'Autreaux B, Tucker NP, Dixon R, and Spiro S. A nonhaem iron centre in the transcription factor NorR senses nitric oxide. Nature 437: 769-772, 2005. (Pubitemid 41486549)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 769-772
    • D'Autreaux, B.1    Tucker, N.P.2    Dixon, R.3    Spiro, S.4
  • 13
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • Ding H and Demple B. In vivo kinetics of a redox-regulated transcriptional switch. Proc Natl Acad Sci U S A 94: 8445-8449, 1997.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 14
    • 67650543834 scopus 로고    scopus 로고
    • Regulation of quinone oxidoreductase by the redox-sensing transcriptional regulator QorR in Corynebacterium glutamicum
    • Ehira S, Ogino H, Teramoto H, Inui M, and Yukawa H. Regulation of quinone oxidoreductase by the redox-sensing transcriptional regulator QorR in Corynebacterium glutamicum. J Biol Chem 284: 16736-16742, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 16736-16742
    • Ehira, S.1    Ogino, H.2    Teramoto, H.3    Inui, M.4    Yukawa, H.5
  • 15
    • 62549099131 scopus 로고    scopus 로고
    • Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro
    • Eiamphungporn W, Soonsanga S, Lee JW, and Helmann JD. Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro. Nucleic Acids Res 37: 1174-1181, 2009.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1174-1181
    • Eiamphungporn, W.1    Soonsanga, S.2    Lee, J.W.3    Helmann, J.D.4
  • 16
    • 33645858540 scopus 로고    scopus 로고
    • Regulation of virulence by members of the MarR/SlyA family
    • Ellison DW and Miller VL. Regulation of virulence by members of the MarR/SlyA family. Curr Opin Microbiol 9: 153-159, 2006.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 153-159
    • Ellison, D.W.1    Miller, V.L.2
  • 17
    • 21244441564 scopus 로고    scopus 로고
    • PpsR: A multifaceted regulator of photosynthesis gene expression in purple bacteria
    • DOI 10.1111/j.1365-2958.2005.04655.x
    • Elsen S, Jaubert M, Pignol D, and Giraud E. PpsR: a multi-faceted regulator of photosynthesis gene expression in purple bacteria. Mol Microbiol 57: 17-26, 2005. (Pubitemid 40896594)
    • (2005) Molecular Microbiology , vol.57 , Issue.1 , pp. 17-26
    • Elsen, S.1    Jaubert, M.2    Pignol, D.3    Giraud, E.4
  • 18
    • 2942558361 scopus 로고    scopus 로고
    • RegB/RegA, a highly conserved redox-responding global two-component regulatory system
    • DOI 10.1128/MMBR.68.2.263-279.2004
    • Elsen S, Swem LR, Swem DL, and Bauer CE. RegB/RegA, a highly conserved redox-responding global two-component regulatory system. Microbiol Mol Biol Rev 68: 263-279, 2004. (Pubitemid 38756865)
    • (2004) Microbiology and Molecular Biology Reviews , vol.68 , Issue.2 , pp. 263-279
    • Elsen, S.1    Swem, L.R.2    Swem, D.L.3    Bauer, C.E.4
  • 19
    • 76049119067 scopus 로고    scopus 로고
    • A nitric oxide/cysteine interaction mediates the activation of soluble guanylate cyclase
    • Fernhoff NB, Derbyshire ER, and Marletta MA. A nitric oxide/cysteine interaction mediates the activation of soluble guanylate cyclase. Proc Natl Acad Sci U S A 106: 21602-21607, 2009.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21602-21607
    • Fernhoff, N.B.1    Derbyshire, E.R.2    Marletta, M.A.3
  • 20
    • 77950887186 scopus 로고    scopus 로고
    • Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation
    • Fourquet S, Guerois R, Biard D, and Toledano MB. Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation. J Biol Chem 285: 8463-8471, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 8463-8471
    • Fourquet, S.1    Guerois, R.2    Biard, D.3    Toledano, M.B.4
  • 21
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • DOI 10.1128/JB.183.14.4134-4141.2001
    • Fuangthong M, Atichartpongkul S, Mongkolsuk S, and Helmann JD. OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J Bacteriol 183: 4134-4141, 2001. (Pubitemid 32568063)
    • (2001) Journal of Bacteriology , vol.183 , Issue.14 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4
  • 25
    • 60849112564 scopus 로고    scopus 로고
    • The YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis of Spx
    • Garg SK, Kommineni S, Henslee L, Zhang Y, and Zuber P. The YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis of Spx. J Bacteriol 191: 1268-1277, 2009.
    • (2009) J Bacteriol , vol.191 , pp. 1268-1277
    • Garg, S.K.1    Kommineni, S.2    Henslee, L.3    Zhang, Y.4    Zuber, P.5
  • 26
    • 0036804709 scopus 로고    scopus 로고
    • BLUF: A novel FAD-binding domain involved in sensory transduction in microorganisms
    • DOI 10.1016/S0968-0004(02)02181-3, PII S0968000402021813
    • Gomelsky M and Klug G. BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms. Trends Biochem Sci 27: 497-500, 2002. (Pubitemid 35279589)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 497-500
    • Gomelsky, M.1    Klug, G.2
  • 27
    • 57649133948 scopus 로고    scopus 로고
    • Dual roles of an essential cysteine residue in activity of a redox-regulated bacterial transcriptional activator
    • Gupta N and Ragsdale SW. Dual roles of an essential cysteine residue in activity of a redox-regulated bacterial transcriptional activator. J Biol Chem 283: 28721-28728, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 28721-28728
    • Gupta, N.1    Ragsdale, S.W.2
  • 29
  • 30
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: Oxidatively modified proteins in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04845.x
    • Hochgrafe F, Mostertz J, Albrecht D, and Hecker M. Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis. Mol Microbiol 58: 409-425, 2005. (Pubitemid 41476158)
    • (2005) Molecular Microbiology , vol.58 , Issue.2 , pp. 409-425
    • Hochgrafe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4
  • 31
    • 34548819035 scopus 로고    scopus 로고
    • S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress
    • Hochgrafe F, Mostertz J, Pother DC, Becher D, Helmann JD, and Hecker M. S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J Biol Chem 282: 25981-25985, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 25981-25985
    • Hochgrafe, F.1    Mostertz, J.2    Pother, D.C.3    Becher, D.4    Helmann, J.D.5    Hecker, M.6
  • 32
    • 25844514282 scopus 로고    scopus 로고
    • Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family
    • DOI 10.1016/j.molcel.2005.09.013, PII S1097276505016345
    • Hong M, Fuangthong M, Helmann JD, and Brennan RG. Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol Cell 20: 131-141, 2005. (Pubitemid 41396568)
    • (2005) Molecular Cell , vol.20 , Issue.1 , pp. 131-141
    • Hong, M.1    Fuangthong, M.2    Helmann, J.D.3    Brennan, R.G.4
  • 33
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of Oxidative Damage
    • DOI 10.1146/annurev.micro.57.030502.090938
    • Imlay JA. Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418, 2003. (Pubitemid 37392949)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 34
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA. Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77: 755-776, 2008.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 35
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • DOI 10.1046/j.1365-2443.2003.00640.x
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, O'Connor T, and Yamamoto M. Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cells 8: 379-391, 2003. (Pubitemid 36504013)
    • (2003) Genes to Cells , vol.8 , Issue.4 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 39
  • 40
    • 34548515549 scopus 로고    scopus 로고
    • Glutathione-dependent alcohol dehydrogenase AdhC is required for defense against nitrosative stress in Haemophilus influenzae
    • DOI 10.1128/IAI.00487-07
    • Kidd SP, Jiang D, Jennings MP, and McEwan AG. Glutathione-dependent alcohol dehydrogenase AdhC is required for defense against nitrosative stress in Haemophilus influenzae. Infect Immun 75: 4506-4513, 2007. (Pubitemid 47378110)
    • (2007) Infection and Immunity , vol.75 , Issue.9 , pp. 4506-4513
    • Kidd, S.P.1    Jiang, D.2    Jennings, M.P.3    McEwan, A.G.4
  • 41
    • 25144450560 scopus 로고    scopus 로고
    • NmIR of Neisseria gonorrhoeae: A novel redox responsive transcription factor from the MerR family
    • DOI 10.1111/j.1365-2958.2005.04773.x
    • Kidd SP, Potter AJ, Apicella MA, Jennings MP, and McEwan AG. NmlR of Neisseria gonorrhoeae: a novel redox responsive transcription factor from the MerR family. Mol Microbiol 57: 1676-1689, 2005. (Pubitemid 41337395)
    • (2005) Molecular Microbiology , vol.57 , Issue.6 , pp. 1676-1689
    • Kidd, S.P.1    Potter, A.J.2    Apicella, M.A.3    Jennings, M.P.4    McEwan, A.G.5
  • 42
    • 70350135937 scopus 로고    scopus 로고
    • Positive and negative feedback regulatory loops of thiol-oxidative stress response mediated by an unstable isoform of sigmaR in actinomycetes
    • Kim MS, Hahn MY, Cho Y, Cho SN, and Roe JH. Positive and negative feedback regulatory loops of thiol-oxidative stress response mediated by an unstable isoform of sigmaR in actinomycetes. Mol Microbiol 73: 815-825, 2009.
    • (2009) Mol Microbiol , vol.73 , pp. 815-825
    • Kim, M.S.1    Hahn, M.Y.2    Cho, Y.3    Cho, S.N.4    Roe, J.H.5
  • 43
    • 33748961329 scopus 로고    scopus 로고
    • Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA
    • DOI 10.1007/s11120-006-9086-4
    • Kim SK, Mason JT, Knaff DB, Bauer CE, and Setterdahl AT. Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA. Photosynth Res 89: 89-98, 2006. (Pubitemid 44440487)
    • (2006) Photosynthesis Research , vol.89 , Issue.2 , pp. 89-98
    • Kim, S.-K.1    Mason, J.T.2    Knaff, D.B.3    Bauer, C.E.4    Setterdahl, A.T.5
  • 45
    • 0344153756 scopus 로고    scopus 로고
    • Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: Exploiting the metabolic spectrum by controlling alternative gene programs
    • DOI 10.1016/S0168-6445(03)00066-4
    • Korner H, Sofia HJ, and Zumft WG. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol Rev 27: 559-592, 2003. (Pubitemid 37456858)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.5 , pp. 559-592
    • Korner, H.1    Sofia, H.J.2    Zumft, W.G.3
  • 46
    • 70349456641 scopus 로고    scopus 로고
    • Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex
    • Lamour V, Westblade LF, Campbell EA, and Darst SA. Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex. J Struct Biol 168: 352-356, 2009.
    • (2009) J Struct Biol , vol.168 , pp. 352-356
    • Lamour, V.1    Westblade, L.F.2    Campbell, E.A.3    Darst, S.A.4
  • 48
  • 49
    • 33645037891 scopus 로고    scopus 로고
    • 2by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation. Nature 440: 363-367, 2006.
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 51
    • 38849183395 scopus 로고    scopus 로고
    • Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2008.06110.x
    • Leelakriangsak M, Huyen NT, Towe S, van Duy N, Becher D, Hecker M, Antelmann H, and Zuber P. Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis. Mol Microbiol 67: 1108-1124, 2008. (Pubitemid 351207337)
    • (2008) Molecular Microbiology , vol.67 , Issue.5 , pp. 1108-1124
    • Leelakriangsak, M.1    Huyen, N.T.T.2    Towe, S.3    Van, D.N.4    Becher, D.5    Hecker, M.6    Antelmann, H.7    Zuber, P.8
  • 52
    • 33947377513 scopus 로고    scopus 로고
    • 3 promoter by repressors PerR and YodB in Bacillus subtilis
    • DOI 10.1128/JB.01520-06
    • Leelakriangsak M, Kobayashi K, and Zuber P. Dual negative control of spx transcription initiation from the P3 promoter by repressors PerR and YodB in Bacillus subtilis. J Bacteriol 189: 1736-1744, 2007. (Pubitemid 46446136)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1736-1744
    • Leelakriangsak, M.1    Kobayashi, K.2    Zuber, P.3
  • 55
    • 0141645618 scopus 로고    scopus 로고
    • The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor
    • DOI 10.1016/j.jmb.2003.08.038
    • Li W, Bottrill AR, Bibb MJ, Buttner MJ, Paget MS, and Kleanthous C. The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor. J Mol Biol 333: 461-472, 2003. (Pubitemid 37188585)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.2 , pp. 461-472
    • Li, W.1    Bottrill, A.R.2    Bibb, M.J.3    Buttner, M.J.4    Paget, M.S.B.5    Kleanthous, C.6
  • 58
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • DOI 10.1016/S0092-8674(02)00876-0
    • Masuda S and Bauer CE. AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. Cell 110: 613-623, 2002. (Pubitemid 35247841)
    • (2002) Cell , vol.110 , Issue.5 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 60
    • 34249726089 scopus 로고    scopus 로고
    • Transcriptional activation by CprK1 is regulated by protein structural changes induced by effector binding and redox state
    • DOI 10.1074/jbc.M611177200
    • Mazon H, Gabor K, Leys D, Heck AJ, van der Oost J, and van den Heuvel RH. Transcriptional activation by CprK1 is regulated by protein structural changes induced by effector binding and redox state. J Biol Chem 282: 11281-11290, 2007. (Pubitemid 47100756)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11281-11290
    • Mazon, H.1    Gabor, K.2    Leys, D.3    Heck, A.J.R.4    Van, D.O.J.5    Van, D.H.R.H.H.6
  • 62
    • 77952518664 scopus 로고    scopus 로고
    • Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit
    • Nakano MM, Lin A, Zuber CS, Newberry KJ, Brennan RG, and Zuber P. Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit. PLoS One 5: e8664, 2010.
    • (2010) PLoS One , vol.5
    • Nakano, M.M.1    Lin, A.2    Zuber, C.S.3    Newberry, K.J.4    Brennan, R.G.5    Zuber, P.6
  • 64
    • 36248933266 scopus 로고    scopus 로고
    • Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR
    • DOI 10.1016/j.molcel.2007.09.016, PII S1097276507006284
    • Newberry KJ, Fuangthong M, Panmanee W, Mongkolsuk S, and Brennan RG. Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR. Mol Cell 28: 652-664, 2007. (Pubitemid 350137793)
    • (2007) Molecular Cell , vol.28 , Issue.4 , pp. 652-664
    • Newberry, K.J.1    Fuangthong, M.2    Panmanee, W.3    Mongkolsuk, S.4    Brennan, R.G.5
  • 65
    • 27644512305 scopus 로고    scopus 로고
    • Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase
    • DOI 10.1073/pnas.0506592102
    • Newberry KJ, Nakano S, Zuber P, and Brennan RG. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc Natl Acad Sci U S A 102: 15839-15844, 2005. (Pubitemid 41552829)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.44 , pp. 15839-15844
    • Newberry, K.J.1    Nakano, S.2    Zuber, P.3    Brennan, R.G.4
  • 66
    • 51949098757 scopus 로고    scopus 로고
    • Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria
    • Newton GL, Buchmeier N, and Fahey RC. Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria. Microbiol Mol Biol Rev 72: 471-494, 2008.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 471-494
    • Newton, G.L.1    Buchmeier, N.2    Fahey, R.C.3
  • 67
    • 42549162094 scopus 로고    scopus 로고
    • Rand the thiol redox sensor anti-sigma factor RsrA
    • DOI 10.1111/j.1365-2958.2008.06222.x
    • Newton GL and Fahey RC. Regulation of mycothiol metabolism by sigma(R) and the thiol redox sensor anti-sigma factor RsrA. Mol Microbiol 68: 805-809, 2008. (Pubitemid 351581072)
    • (2008) Molecular Microbiology , vol.68 , Issue.4 , pp. 805-809
    • Newton, G.L.1    Fahey, R.C.2
  • 69
    • 67649402187 scopus 로고    scopus 로고
    • The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
    • Nguyen T, Nioi P, and Pickett CB. The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress. J Biol Chem 284: 13291-13295, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 13291-13295
    • Nguyen, T.1    Nioi, P.2    Pickett, C.B.3
  • 70
    • 60349101109 scopus 로고    scopus 로고
    • Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: Control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR)
    • Nguyen TT, Eiamphungporn W, Mader U, Liebeke M, Lalk M, Hecker M, Helmann JD, and Antelmann H. Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR). Mol Microbiol 71: 876-894, 2009.
    • (2009) Mol Microbiol , vol.71 , pp. 876-894
    • Nguyen, T.T.1    Eiamphungporn, W.2    Mader, U.3    Liebeke, M.4    Lalk, M.5    Hecker, M.6    Helmann, J.D.7    Antelmann, H.8
  • 71
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-Based Regulatory Switches
    • DOI 10.1146/annurev.genet.37.110801.142538
    • Paget MS and Buttner MJ. Thiol-based regulatory switches. Annu Rev Genet 37: 91-121, 2003. (Pubitemid 38041422)
    • (2003) Annual Review of Genetics , vol.37 , pp. 91-121
    • Paget, M.S.B.1    Buttner, M.J.2
  • 72
    • 0036032183 scopus 로고    scopus 로고
    • OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli
    • DOI 10.1046/j.1365-2958.2002.03116.x
    • Panmanee W, Vattanaviboon P, Eiamphungporn W, Whangsuk W, Sallabhan R, and Mongkolsuk S. OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli. Mol Microbiol 45: 1647-1654, 2002. (Pubitemid 35231980)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1647-1654
    • Panmanee, W.1    Vattanaviboon, P.2    Eiamphungporn, W.3    Whangsuk, W.4    Sallabhan, R.5    Mongkolsuk, S.6
  • 73
    • 32444439989 scopus 로고    scopus 로고
    • Novel organic hydroperoxide-sensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress
    • DOI 10.1128/JB.188.4.1389-1395.2006
    • Panmanee W, Vattanaviboon P, Poole LB, and Mongkolsuk S. Novel organic hydroperoxide-sensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress. J Bacteriol 188: 1389-1395, 2006. (Pubitemid 43228671)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1389-1395
    • Panmanee, W.1    Vattanaviboon, P.2    Poole, L.B.3    Mongkolsuk, S.4
  • 74
    • 42549139480 scopus 로고    scopus 로고
    • Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor
    • Park JH and Roe JH. Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor. Mol Microbiol 68: 861-870, 2008.
    • (2008) Mol Microbiol , vol.68 , pp. 861-870
    • Park, J.H.1    Roe, J.H.2
  • 75
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen CE and Carroll KS. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 5: 47-62, 2010.
    • (2010) ACS Chem Biol , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 76
    • 34047158876 scopus 로고    scopus 로고
    • Zinc-promoted alkyl transfer: A new role for zinc
    • DOI 10.1016/j.cbpa.2007.02.038, PII S1367593107000324
    • Penner-Hahn J. Zinc-promoted alkyl transfer: a new role for zinc. Curr Opin Chem Biol 11: 166-171, 2007. (Pubitemid 46528373)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.2 , pp. 166-171
    • Penner-Hahn, J.1
  • 78
    • 69949138465 scopus 로고    scopus 로고
    • Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus
    • Poor CB, Chen PR, Duguid E, Rice PA, and He C. Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus. J Biol Chem 284: 23517-23524, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 23517-23524
    • Poor, C.B.1    Chen, P.R.2    Duguid, E.3    Rice, P.A.4    He, C.5
  • 79
    • 33748757442 scopus 로고    scopus 로고
    • Transcriptional activation of dehalorespiration: Identification of redox-active cysteines regulating dimerization and DNA binding
    • DOI 10.1074/jbc.M602158200
    • Pop SM, Gupta N, Raza AS, and Ragsdale SW. Transcriptional activation of dehalorespiration: identification of redox-active cysteines regulating dimerization and DNA binding. J Biol Chem 281: 26382-26390, 2006. (Pubitemid 44401846)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26382-26390
    • Pop, S.M.1    Gupta, N.2    Raza, A.S.3    Ragsdale, S.W.4
  • 80
    • 9644265299 scopus 로고    scopus 로고
    • Regulation of anaerobic dehalorespiration by the transcriptional activator CprK
    • DOI 10.1074/jbc.M409435200
    • Pop SM, Kolarik RJ, and Ragsdale SW. Regulation of anaerobic dehalorespiration by the transcriptional activator CprK. J Biol Chem 279: 49910-49918, 2004. (Pubitemid 39577799)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 49910-49918
    • Pop, S.M.1    Kolarik, R.J.2    Ragsdale, S.W.3
  • 82
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • DOI 10.1038/nature01680
    • Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423: 769-773, 2003. (Pubitemid 36735701)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.-C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 83
    • 0023916658 scopus 로고
    • Sequences, sequences, and sequences
    • Sanger F. Sequences, sequences, and sequences. Annu Rev Biochem 57: 1-28, 1988.
    • (1988) Annu Rev Biochem , vol.57 , pp. 1-28
    • Sanger, F.1
  • 84
    • 70349482669 scopus 로고    scopus 로고
    • Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies
    • Seo YH and Carroll KS. Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies. Proc Natl Acad Sci U S A 106: 16163-16168, 2009.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16163-16168
    • Seo, Y.H.1    Carroll, K.S.2
  • 85
    • 50249123949 scopus 로고    scopus 로고
    • Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor
    • Soonsanga S, Lee JW, and Helmann JD. Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor. J Bacteriol 190: 5738-5745, 2008.
    • (2008) J Bacteriol , vol.190 , pp. 5738-5745
    • Soonsanga, S.1    Lee, J.W.2    Helmann, J.D.3
  • 86
    • 42549107897 scopus 로고    scopus 로고
    • Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR
    • DOI 10.1111/j.1365-2958.2008.06200.x
    • Soonsanga S, Lee JW, and Helmann JD. Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR. Mol Microbiol 68: 978-986, 2008. (Pubitemid 351581061)
    • (2008) Molecular Microbiology , vol.68 , Issue.4 , pp. 978-986
    • Soonsanga, S.1    Lee, J.-W.2    Helmann, J.D.3
  • 87
    • 39149119282 scopus 로고    scopus 로고
    • A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence
    • Stroeher UH, Kidd SP, Stafford SL, Jennings MP, Paton JC, and McEwan AG. A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence. J Infect Dis 196: 1820-1826, 2007.
    • (2007) J Infect Dis , vol.196 , pp. 1820-1826
    • Stroeher, U.H.1    Kidd, S.P.2    Stafford, S.L.3    Jennings, M.P.4    Paton, J.C.5    McEwan, A.G.6
  • 88
    • 0034944405 scopus 로고    scopus 로고
    • Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves ohrR, a novel organic peroxide-inducible negative regulator, and posttranscriptional modifications
    • DOI 10.1128/JB.183.15.4405-4412.2001
    • Sukchawalit R, Loprasert S, Atichartpongkul S, and Mongkolsuk S. Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-inducible negative regulator, and posttranscriptional modifications. J Bacteriol 183: 4405-4412, 2001. (Pubitemid 32645989)
    • (2001) Journal of Bacteriology , vol.183 , Issue.15 , pp. 4405-4412
    • Sukchawalit, R.1    Loprasert, S.2    Atichartpongkul, S.3    Mongkolsuk, S.4
  • 89
    • 33646594462 scopus 로고    scopus 로고
    • Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB
    • DOI 10.1074/jbc.M509687200
    • Swem LR, Gong X, Yu CA, and Bauer CE. Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB. J Biol Chem 281: 6768-6775, 2006. (Pubitemid 43847613)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6768-6775
    • Swem, L.R.1    Gong, X.2    Yu, C.-A.3    Bauer, C.E.4
  • 90
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • DOI 10.1038/nature01681
    • van Montfort RL, Congreve M, Tisi D, Carr R, and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423: 773-777, 2003. (Pubitemid 36735702)
    • (2003) Nature , vol.423 , Issue.6941 , pp. 773-777
    • Van, M.R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 91
    • 69449090357 scopus 로고    scopus 로고
    • Cysteine modification of a specific repressor protein controls the translational status of nucleus-encoded LHCII mRNAs in Chlamydomonas
    • Wobbe L, Blifernez O, Schwarz C, Mussgnug JH, Nickelsen J, and Kruse O. Cysteine modification of a specific repressor protein controls the translational status of nucleus-encoded LHCII mRNAs in Chlamydomonas. Proc Natl Acad Sci U S A 106: 13290-13295, 2009.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13290-13295
    • Wobbe, L.1    Blifernez, O.2    Schwarz, C.3    Mussgnug, J.H.4    Nickelsen, J.5    Kruse, O.6
  • 92
    • 4344562921 scopus 로고    scopus 로고
    • Structural basis for redox regulation of Yap1 transcription factor localization
    • DOI 10.1038/nature02790
    • Wood MJ, Storz G, and Tjandra N. Structural basis for redox regulation of Yap1 transcription factor localization. Nature 430: 917-921, 2004. (Pubitemid 39119222)
    • (2004) Nature , vol.430 , Issue.7002 , pp. 917-921
    • Wood, M.J.1    Storz, G.2    Tjandra, N.3
  • 93
    • 22144480660 scopus 로고    scopus 로고
    • HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04702.x
    • Yurimoto H, Hirai R, Matsuno N, Yasueda H, Kato N, and Sakai Y. HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis. Mol Microbiol 57: 511-519, 2005. (Pubitemid 40979349)
    • (2005) Molecular Microbiology , vol.57 , Issue.2 , pp. 511-519
    • Yurimoto, H.1    Hirai, R.2    Matsuno, N.3    Yasueda, H.4    Kato, N.5    Sakai, Y.6
  • 94
    • 33745837091 scopus 로고    scopus 로고
    • Assignment of the zinc ligands in RsrA, a redox-sensing ZAS protein from Streptomyces coelicolor
    • DOI 10.1021/bi060711v
    • Zdanowski K, Doughty P, Jakimowicz P, O'Hara L, Buttner MJ, Paget MS, and Kleanthous C. Assignment of the zinc ligands in RsrA, a redox-sensing ZAS protein from Streptomyces coelicolor. Biochemistry 45: 8294-8300, 2006. (Pubitemid 44036535)
    • (2006) Biochemistry , vol.45 , Issue.27 , pp. 8294-8300
    • Zdanowski, K.1    Doughty, P.2    Jakimowicz, P.3    O'Hara, L.4    Buttner, M.J.5    Paget, M.S.B.6    Kleanthous, C.7
  • 95
    • 1642352469 scopus 로고    scopus 로고
    • Spx-RNA polymerase interaction and global transcriptional control during oxidative stress
    • Zuber P. Spx-RNA polymerase interaction and global transcriptional control during oxidative stress. J Bacteriol 186: 1911-1918, 2004.
    • (2004) J Bacteriol , vol.186 , pp. 1911-1918
    • Zuber, P.1
  • 96
    • 70349547204 scopus 로고    scopus 로고
    • Management of oxidative stress in Bacillus
    • Zuber P. Management of oxidative stress in Bacillus. Annu Rev Microbiol 63: 575-597, 2009.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 575-597
    • Zuber, P.1


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