메뉴 건너뛰기




Volumn 10, Issue 17, 2010, Pages 3155-3164

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

Author keywords

Disulfide bond formation; Electrophiles; Microbiology; Redox sensing; YodB

Indexed keywords

2 METHYLHYDROQUINONE; BACTERIAL PROTEIN; DIAMIDE; DISULFIDE; OLIGONUCLEOTIDE; PROTEIN YODB; QUINONE DERIVATIVE; REPRESSOR PROTEIN; THIOL; UNCLASSIFIED DRUG;

EID: 77956131582     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000230     Document Type: Article
Times cited : (37)

References (38)
  • 1
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget, M. S., Buttner, M. J., Thiol-based regulatory switches. Annu. Rev. Genet. 2003, 37, 91-121.
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 2
    • 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. 2004, 14, 679-686. (Pubitemid 39592578)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.6 , pp. 679-686
    • Barford, D.1
  • 4
    • 33845648094 scopus 로고    scopus 로고
    • Redox regulation of neuronal survival mediated by electrophilic compounds
    • DOI 10.1016/j.tins.2006.11.004, PII S0166223606002670
    • Satoh, T., Lipton, S. A., Redox regulation of neuronal survival mediated by electrophilic compounds. Trends Neurosci. 2007, 30, 37-45. (Pubitemid 44960491)
    • (2007) Trends in Neurosciences , vol.30 , Issue.1 , pp. 37-45
    • Satoh, T.1    Lipton, S.A.2
  • 5
    • 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, T. T., Eiamphungporn, W., Mäder, U., Liebeke, M. et al., 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. 2009, 71, 876-894.
    • (2009) Mol. Microbiol. , vol.71 , pp. 876-894
    • Nguyen, T.T.1    Eiamphungporn, W.2    Mäder, U.3    Liebeke, M.4
  • 7
    • 36248990256 scopus 로고    scopus 로고
    • Characterization and quantification of reversible redox sites in humic substances
    • DOI 10.1021/es071389u
    • Ratasuk, N., Nanny, M. A., Characterization and quantification of reversible redox sites in humic substances. Environ. Sci. Technol. 2007, 41, 7844-7850. (Pubitemid 350133327)
    • (2007) Environmental Science and Technology , vol.41 , Issue.22 , pp. 7844-7850
    • Ratasuk, N.1    Nanny, M.A.2
  • 8
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: Oxidatively modified proteins in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2005.04845.x
    • Hochgräfe, F., Mostertz, J., Albrecht, D., Hecker, M., Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis. Mol. Microbiol. 2005, 58, 409-425. (Pubitemid 41476158)
    • (2005) Molecular Microbiology , vol.58 , Issue.2 , pp. 409-425
    • Hochgrafe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4
  • 9
    • 34548819035 scopus 로고    scopus 로고
    • S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress
    • DOI 10.1074/jbc.C700105200
    • Hochgräfe, F., Mostertz, J., Pöther, D. C., Becher, D. et al., S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J. Biol. Chem. 2007, 282, 25981-25985. (Pubitemid 47443757)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 25961-25985
    • Hochgrafe, F.1    Mostertz, J.2    Pother, D.-C.3    Becher, D.4    Helmann, J.D.5    Hecker, M.6
  • 10
    • 72449174430 scopus 로고    scopus 로고
    • Diamide triggers mainly S Thiolations in the cytoplasmic proteomes of Bacillus subtilis and Staphylococcus aureus
    • Pöther, D. C., Liebeke, M., Hochgräfe, F., Antelmann, H. et al., Diamide triggers mainly S Thiolations in the cytoplasmic proteomes of Bacillus subtilis and Staphylococcus aureus. J. Bacteriol. 2009, 191, 7520-7530.
    • (2009) J. Bacteriol. , vol.191 , pp. 7520-7530
    • Pöther, D.C.1    Liebeke, M.2    Hochgräfe, F.3    Antelmann, H.4
  • 11
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien, P. J., Molecular mechanisms of quinone cytotoxicity. Chem. Biol. Interact. 1991, 80, 1-41.
    • (1991) Chem. Biol. Interact. , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 14
    • 50049125078 scopus 로고    scopus 로고
    • Depletion of thiol-containing proteins in response to quinones in Bacillus subtilis
    • Liebeke, M., Pöther, D. C., van Duy, N., Albrecht, D. et al., Depletion of thiol-containing proteins in response to quinones in Bacillus subtilis. Mol. Microbiol. 2008, 69, 1513-1529.
    • (2008) Mol. Microbiol. , vol.69 , pp. 1513-1529
    • Liebeke, M.1    Pöther, D.C.2    Van Duy, N.3    Albrecht, D.4
  • 15
    • 13144257719 scopus 로고    scopus 로고
    • Redox-sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx
    • Nakano, S., Erwin, K. N., Ralle, M., Zuber, P., Redox-sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx. Mol. Microbiol. 2005, 55, 498-510.
    • (2005) Mol. Microbiol. , vol.55 , pp. 498-510
    • Nakano, S.1    Erwin, K.N.2    Ralle, M.3    Zuber, P.4
  • 16
    • 0344392193 scopus 로고    scopus 로고
    • Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis
    • Nakano, S., Kuster-Schock, E., Grossman, A. D., Zuber, P., Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 2003, 100, 13603-13608.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13603-13608
    • Nakano, S.1    Kuster-Schock, E.2    Grossman, A.D.3    Zuber, P.4
  • 17
    • 38849183395 scopus 로고    scopus 로고
    • Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis
    • Leelakriangsak, M., Huyen, N. T., Töwe, S., van Duy, N. et al., Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis. Mol. Microbiol. 2008, 67, 1108-1124.
    • (2008) Mol. Microbiol. , vol.67 , pp. 1108-1124
    • Leelakriangsak, M.1    Huyen, N.T.2    Töwe, S.3    Van Duy, N.4
  • 18
    • 33947377513 scopus 로고    scopus 로고
    • Dual negative control of spx transcription initiation from the P3 promoter by repressors PerR and YodB in Bacillus subtilis
    • Leelakriangsak, M., Kobayashi, K., Zuber, P., Dual negative control of spx transcription initiation from the P3 promoter by repressors PerR and YodB in Bacillus subtilis. J. Bacteriol. 2007, 189, 1736-1744.
    • (2007) J. Bacteriol. , vol.189 , pp. 1736-1744
    • Leelakriangsak, M.1    Kobayashi, K.2    Zuber, P.3
  • 19
    • 33947420461 scopus 로고    scopus 로고
    • Transcription from the P3 promoter of the Bacillus subtilis spx gene is induced in response to disulfide stress
    • Leelakriangsak, M., Zuber, P., Transcription from the P3 promoter of the Bacillus subtilis spx gene is induced in response to disulfide stress. J. Bacteriol. 2007, 189, 1727-1735.
    • (2007) J. Bacteriol. , vol.189 , pp. 1727-1735
    • Leelakriangsak, M.1    Zuber, P.2
  • 20
    • 34548677758 scopus 로고    scopus 로고
    • The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis
    • Töwe, S., Leelakriangsak, M., Kobayashi, K., Van Duy, N. et al., The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis. Mol. Microbiol. 2007, 66, 40-54.
    • (2007) Mol. Microbiol. , vol.66 , pp. 40-54
    • Töwe, S.1    Leelakriangsak, M.2    Kobayashi, K.3    Van Duy, N.4
  • 21
    • 39649108459 scopus 로고    scopus 로고
    • Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis
    • Antelmann, H., Hecker, M., Zuber, P., Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis. Expert Rev. Proteomics 2008, 5, 77-90.
    • (2008) Expert Rev. Proteomics , vol.5 , pp. 77-90
    • Antelmann, H.1    Hecker, M.2    Zuber, P.3
  • 22
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk, S., Helmann, J. D., Regulation of inducible peroxide stress responses. Mol. Microbiol. 2002, 45, 9-15.
    • (2002) Mol. Microbiol. , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 23
    • 0036096988 scopus 로고    scopus 로고
    • The repressor for an organic peroxideinducible operon is uniquely regulated at multiple levels
    • Mongkolsuk, S., Panmanee, W., Atichartpongkul, S., Vattanaviboon, P. et al., The repressor for an organic peroxideinducible operon is uniquely regulated at multiple levels. Mol. Microbiol. 2002, 44, 793-802.
    • (2002) Mol. Microbiol. , vol.44 , pp. 793-802
    • Mongkolsuk, S.1    Panmanee, W.2    Atichartpongkul, S.3    Vattanaviboon, P.4
  • 24
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • Fuangthong, M., Atichartpongkul, S., Mongkolsuk, S., Helmann, J. D., OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J. Bacteriol. 2001, 183, 4134-4141.
    • (2001) J. Bacteriol. , vol.183 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4
  • 25
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M., Helmann, J. D., The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl. Acad. Sci. USA 2002, 99, 6690-6695.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 26
    • 34547399134 scopus 로고    scopus 로고
    • A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR
    • Lee, J. W., Soonsanga, S., Helmann, J. D., A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR. Proc. Natl. Acad. Sci. USA 2007, 104, 8743-8748.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8743-8748
    • Lee, J.W.1    Soonsanga, S.2    Helmann, J.D.3
  • 27
    • 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. et al., OhrR, a transcription repressor that senses and responds to changes in organic peroxide levels in Xanthomonas campestris pv. phaseoli. Mol. Microbiol. 2002, 45, 1647-1654. (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
  • 28
    • 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, L. B., Mongkolsuk, S., Novel organic hydroperoxide-sensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress. J. Bacteriol. 2006, 188, 1389-1395. (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
  • 29
    • 42549107897 scopus 로고    scopus 로고
    • Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR
    • Soonsanga, S., Lee, J. W., Helmann, J. D., Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR. Mol. Microbiol. 2008, 68, 978-986.
    • (2008) Mol. Microbiol. , vol.68 , pp. 978-986
    • Soonsanga, S.1    Lee, J.W.2    Helmann, J.D.3
  • 30
    • 50249123949 scopus 로고    scopus 로고
    • Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor
    • Soonsanga, S., Lee, J. W., Helmann, J. D., Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor. J. Bacteriol. 2008, 190, 5738-5745.
    • (2008) J. Bacteriol. , vol.190 , pp. 5738-5745
    • Soonsanga, S.1    Lee, J.W.2    Helmann, J.D.3
  • 32
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guerout-Fleury, A. M., Shazand, K., Frandsen, N., Stragier, P., Antibiotic-resistance cassettes for Bacillus subtilis. Gene 1995, 167, 335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 33
    • 0027524789 scopus 로고
    • Temporal activation of beta-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • Stülke, J., Hanschke, R., Hecker, M., Temporal activation of beta-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool. J. Gen. Microbiol. 1993, 139, 2041-2045.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2041-2045
    • Stülke, J.1    Hanschke, R.2    Hecker, M.3
  • 34
    • 0026750167 scopus 로고
    • Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis
    • Wetzstein, M., Volker, U., Dedio, J., Lobau, S. et al., Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis. J. Bacteriol. 1992, 174, 3300-3310.
    • (1992) J. Bacteriol. , vol.174 , pp. 3300-3310
    • Wetzstein, M.1    Volker, U.2    Dedio, J.3    Lobau, S.4
  • 35
    • 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
    • Yurimoto, H., Hirai, R., Matsuno, N., Yasueda, H. et al., 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. 2005, 57, 511-519.
    • (2005) Mol. Microbiol. , vol.57 , pp. 511-519
    • Yurimoto, H.1    Hirai, R.2    Matsuno, N.3    Yasueda, H.4
  • 36
    • 34248630834 scopus 로고    scopus 로고
    • Transcriptome and proteome analyses in response to 2-methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems involved in the catabolism of aromatic compounds in Bacillus subtilis
    • Nguyen, V. D., Wolf, C., Mäder, U., Lalk, M. et al., Transcriptome and proteome analyses in response to 2-methylhydroquinone and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems involved in the catabolism of aromatic compounds in Bacillus subtilis. Proteomics 2007, 7, 1391-1408.
    • (2007) Proteomics , vol.7 , pp. 1391-1408
    • Nguyen, V.D.1    Wolf, C.2    Mäder, U.3    Lalk, M.4
  • 37
    • 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., Yukawa, H., Regulation of quinone oxidoreductase by the redox-sensing transcriptional regulator QorR in Corynebacterium glutamicum. J. Biol. Chem. 2009, 284, 16736-16742.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16736-16742
    • Ehira, S.1    Ogino, H.2    Teramoto, H.3    Inui, M.4    Yukawa, H.5
  • 38
    • 77950868171 scopus 로고    scopus 로고
    • Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli
    • Gaballa, A., Newton, G. L., Antelmann, H., Parsonage, D. et al., Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli. Proc. Natl. Acad. Sci. USA 2010, 107, 6482-6486.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6482-6486
    • Gaballa, A.1    Newton, G.L.2    Antelmann, H.3    Parsonage, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.