메뉴 건너뛰기




Volumn 407, Issue 4, 2011, Pages 477-491

Features of Rhodobacter sphaeroides ChrR required for stimuli to promote the dissociation of σe/ChrR complexes

Author keywords

4 (2 pyridylazo) resorcinol; chloramphenicol; ChrR anti domain; ChrR cupin like domain; ChrR ASD; ChrR CLD; Cm; p chloromercuribenzoic acid; PAR; PCMB; t BOOH; t butyl hydroperoxide

Indexed keywords

ALANINE; CHRR PROTEIN; CYSTEINE; GLUTAMIC ACID; HISTIDINE; METALLOPROTEIN; REACTIVE OXYGEN METABOLITE; SINGLET OXYGEN; TERT BUTYL HYDROPEROXIDE; UNCLASSIFIED DRUG; ZINC;

EID: 79952454776     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.01.055     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 0002696602 scopus 로고
    • Oxygen stress and superoxide dismutases
    • Scandalios J.G. Oxygen stress and superoxide dismutases Plant Physiol. 101 1993 7 12
    • (1993) Plant Physiol. , vol.101 , pp. 7-12
    • Scandalios, J.G.1
  • 2
    • 1542313800 scopus 로고    scopus 로고
    • Oxygen intervention in the regulation of gene expression: The photosynthetic bacterial paradigm
    • DOI 10.1007/s00018-003-3242-1
    • Zeilstra-Ryalls J.H., and Kaplan S. Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm Cell. Mol. Life Sci. 61 2004 417 436 (Pubitemid 38316579)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.4 , pp. 417-436
    • Zeilstra-Ryalls, J.H.1    Kaplan, S.2
  • 3
    • 42949144160 scopus 로고    scopus 로고
    • The biology of oxygen
    • Wagner P.D. The biology of oxygen Eur. Respir. J. 31 2008 887 890
    • (2008) Eur. Respir. J. , vol.31 , pp. 887-890
    • Wagner, P.D.1
  • 5
    • 0034676493 scopus 로고    scopus 로고
    • Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology
    • Mates J.M. Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology Toxicology 153 2000 83 104
    • (2000) Toxicology , vol.153 , pp. 83-104
    • Mates, J.M.1
  • 7
    • 0035196519 scopus 로고    scopus 로고
    • Persulfoxide: Key intermediate in reactions of singlet oxygen with sulfides
    • DOI 10.1021/ar0100879
    • Clennan E.L. Persulfoxide: key intermediate in reactions of singlet oxygen with sulfides Acc. Chem. Res. 34 2001 875 884 (Pubitemid 33104941)
    • (2001) Accounts of Chemical Research , vol.34 , Issue.11 , pp. 875-884
    • Clennan, E.L.1
  • 8
    • 3042688696 scopus 로고    scopus 로고
    • Reactive species formed on proteins exposed to singlet oxygen
    • DOI 10.1039/b307576c
    • Davies M.J. Reactive species formed on proteins exposed to singlet oxygen Photochem. Photobiol. Sci. 3 2004 17 25 (Pubitemid 38842660)
    • (2004) Photochemical and Photobiological Sciences , vol.3 , Issue.1 , pp. 17-25
    • Davies, M.J.1
  • 9
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • DOI 10.1016/j.bbapap.2004.08.007, PII S1570963904002183, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Davies M.J. The oxidative environment and protein damage Biochim. Biophys. Acta 1703 2005 93 109 (Pubitemid 40170433)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 93-109
    • Davies, M.J.1
  • 10
    • 1642533553 scopus 로고    scopus 로고
    • Formation of radicals from singlet oxygen produced during photoinhibition of isolated light-harvesting proteins of photosystem II
    • DOI 10.1016/j.bbabio.2003.10.009
    • Rinalducci S., Pedersen J.Z., and Zolla L. Formation of radicals from singlet oxygen produced during photoinhibition of isolated light-harvesting proteins of photosystem II Biochim. Biophys. Acta 1608 2004 63 73 (Pubitemid 38115119)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1608 , Issue.1 , pp. 63-73
    • Rinalducci, S.1    Pedersen, J.Z.2    Zolla, L.3
  • 15
    • 52949112607 scopus 로고    scopus 로고
    • Organization and evolution of the biological response to singlet oxygen stress
    • Dufour Y.S., Landick R., and Donohue T.J. Organization and evolution of the biological response to singlet oxygen stress J. Mol. Biol. 383 2008 713 730
    • (2008) J. Mol. Biol. , vol.383 , pp. 713-730
    • Dufour, Y.S.1    Landick, R.2    Donohue, T.J.3
  • 16
  • 17
    • 34548252292 scopus 로고    scopus 로고
    • A Conserved Structural Module Regulates Transcriptional Responses to Diverse Stress Signals in Bacteria
    • DOI 10.1016/j.molcel.2007.07.009, PII S1097276507004807
    • Campbell E.A., Greenwell R., Anthony J.R., Wang S., Lim L., and Das K. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria Mol. Cell 27 2007 793 805 (Pubitemid 47333225)
    • (2007) Molecular Cell , vol.27 , Issue.5 , pp. 793-805
    • Campbell, E.A.1    Greenwell, R.2    Anthony, J.R.3    Wang, S.4    Lim, L.5    Das, K.6    Sofia, H.J.7    Donohue, T.J.8    Darst, S.A.9
  • 19
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: The most functionally diverse protein superfamily?
    • DOI 10.1016/j.phytochem.2003.08.016
    • Dunwell J.M., Purvis A., and Khuri S. Cupins: the most functionally diverse protein superfamily? Phytochemistry 65 2004 7 17 (Pubitemid 38155888)
    • (2004) Phytochemistry , vol.65 , Issue.1 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 21
    • 0035955551 scopus 로고    scopus 로고
    • The importance of zinc-binding to the function of Rhodobacter sphaeroides ChrR as an anti-sigma factor
    • DOI 10.1006/jmbi.2001.5069
    • Newman J.D., Anthony J.R., and Donohue T.J. The importance of zinc-binding to the function of Rhodobacter sphaeroides ChrR as an anti-sigma factor J. Mol. Biol. 313 2001 485 499 (Pubitemid 33052282)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.3 , pp. 485-499
    • Newman, J.D.1    Anthony, J.R.2    Donohue, T.J.3
  • 22
    • 0035116721 scopus 로고    scopus 로고
    • Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch
    • DOI 10.1046/j.1365-2958.2001.02298.x
    • Paget M.S., Bae J.B., Hahn M.Y., Li W., Kleanthous C., Roe J.H., and Buttner M.J. Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch Mol. Microbiol. 39 2001 1036 1047 (Pubitemid 32176346)
    • (2001) Molecular Microbiology , vol.39 , Issue.4 , pp. 1036-1047
    • Paget, M.S.B.1    Bae, J.-B.2    Hahn, M.-Y.3    Li, W.4    Kleanthous, C.5    Roe, J.-H.6    Buttner, M.J.7
  • 23
    • 0029149516 scopus 로고
    • Characterization of metal binding by a designed protein: Single ligand substitutions at a tetrahedral Cys2His2 site
    • Klemba M., and Regan L. Characterization of metal binding by a designed protein: single ligand substitutions at a tetrahedral Cys2His2 site Biochemistry 34 1995 10094 10100
    • (1995) Biochemistry , vol.34 , pp. 10094-10100
    • Klemba, M.1    Regan, L.2
  • 24
    • 1642494634 scopus 로고    scopus 로고
    • Emission Ratiometric Imaging of Intracellular Zinc: Design of a Benzoxazole Fluorescent Sensor and Its Application in Two-Photon Microscopy
    • DOI 10.1021/ja039073j
    • Taki M., Wolford J.L., and O'Halloran T.V. Emission ratiometric imaging of intracellular zinc: design of a benzoxazole fluorescent sensor and its application in two-photon microscopy J. Am. Chem. Soc. 126 2004 712 713 (Pubitemid 38114344)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.3 , pp. 712-713
    • Taki, M.1    Wolford, J.L.2    O'Halloran, T.V.3
  • 25
    • 0015333007 scopus 로고
    • Stability constant for the zinc-dithiothreitol complex
    • Cornell N.W., and Crivaro K.E. Stability constant for the zinc-dithiothreitol complex Anal. Biochem. 47 1972 203 208
    • (1972) Anal. Biochem. , vol.47 , pp. 203-208
    • Cornell, N.W.1    Crivaro, K.E.2
  • 26
    • 0014409457 scopus 로고
    • Studies on phosphomannose isomerase: II. Characterization as a zinc metalloenzyme
    • Gracy R.W., and Noltmann E.A. Studies on phosphomannose isomerase: II. Characterization as a zinc metalloenzyme J. Biol. Chem. 243 1968 4109 4116
    • (1968) J. Biol. Chem. , vol.243 , pp. 4109-4116
    • Gracy, R.W.1    Noltmann, E.A.2
  • 28
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • DOI 10.1016/S0006-291X(03)00817-9
    • Davies M.J. Singlet oxygen-mediated damage to proteins and its consequences Biochem. Biophys. Res. Commun. 305 2003 761 770 (Pubitemid 36579294)
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , Issue.3 , pp. 761-770
    • Davies, M.J.1
  • 29
    • 0036632772 scopus 로고    scopus 로고
    • Singlet oxygen-mediated protein oxidation: Evidence for the formation of reactive side chain peroxides on tyrosine residues
    • Wright A., Bubb W.A., Hawkins C.L., and Davies M.J. Singlet oxygen-mediated protein oxidation: evidence for the formation of reactive side chain peroxides on tyrosine residues Photochem. Photobiol. 76 2002 35 46
    • (2002) Photochem. Photobiol. , vol.76 , pp. 35-46
    • Wright, A.1    Bubb, W.A.2    Hawkins, C.L.3    Davies, M.J.4
  • 31
    • 0025637021 scopus 로고
    • Carotenoids, tocopherols and thiols as biological singlet molecular oxygen quenchers
    • Di Mascio P., Devasagayam T.P., Kaiser S., and Sies H. Carotenoids, tocopherols and thiols as biological singlet molecular oxygen quenchers Biochem. Soc. Trans. 18 1990 1054 1056
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 1054-1056
    • Di Mascio, P.1    Devasagayam, T.P.2    Kaiser, S.3    Sies, H.4
  • 32
    • 23944469034 scopus 로고    scopus 로고
    • Conformationally induced electrostatic stabilization of persulfoxides: A new suggestion for inhibition of physical quenching of singlet oxygen by remote functional groups
    • DOI 10.1021/ja0525509
    • Clennan E.L., Hightower S.E., and Greer A. Conformationally induced electrostatic stabilization of persulfoxides: a new suggestion for inhibition of physical quenching of singlet oxygen by remote functional groups J. Am. Chem. Soc. 127 2005 11819 11826 (Pubitemid 41208767)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.33 , pp. 11819-11826
    • Clennan, E.L.1    Hightower, S.E.2    Greer, A.3
  • 34
    • 0024403347 scopus 로고
    • Singlet oxygen production by biological systems
    • DOI 10.1016/0009-2797(89)90059-8
    • Kanofsky J.R. Singlet oxygen production by biological systems Chem. Biol. Interact. 70 1989 1 28 (Pubitemid 19161211)
    • (1989) Chemico-Biological Interactions , vol.70 , Issue.1-2 , pp. 1-28
    • Kanofsky, J.R.1
  • 35
    • 1542316790 scopus 로고    scopus 로고
    • Singlet oxygen signaling: From intimate to global
    • 101126/stke2212004pe7
    • Kochevar I. Singlet oxygen signaling: from intimate to global Sci. STKE 2004 2004 pe7 10.1126/stke.2212004pe7
    • (2004) Sci. STKE , vol.2004 , pp. 7
    • Kochevar, I.1
  • 36
    • 10744226907 scopus 로고    scopus 로고
    • Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells
    • Lupinkova L., and Komenda J. Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells Photochem. Photobiol. 79 2004 152 162
    • (2004) Photochem. Photobiol. , vol.79 , pp. 152-162
    • Lupinkova, L.1    Komenda, J.2
  • 37
    • 0026305225 scopus 로고
    • Biological consequences associated with DNA oxidation mediated by singlet oxygen
    • Piette J. Biological consequences associated with DNA oxidation mediated by singlet oxygen J. Photochem. Photobiol. B 11 1991 241 260
    • (1991) J. Photochem. Photobiol. B , vol.11 , pp. 241-260
    • Piette, J.1
  • 38
    • 0033913112 scopus 로고    scopus 로고
    • Singlet oxygen-mediated protein oxidation: Evidence for the formation of reactive peroxides
    • Wright A., Hawkins C.L., and Davies M.J. Singlet oxygen-mediated protein oxidation: evidence for the formation of reactive peroxides Redox Rep. 5 2000 159 161 (Pubitemid 30488529)
    • (2000) Redox Report , vol.5 , Issue.2-3 , pp. 159-161
    • Wright, A.1    Hawkins, C.L.2    Davies, M.J.3
  • 39
    • 21344459291 scopus 로고    scopus 로고
    • Photo-oxidative stress in Rhodobacter sphaeroides: Protective role of carotenoids and expression of selected genes
    • DOI 10.1099/mic.0.027789-0
    • Glaeser J., and Klug G. Photo-oxidative stress in Rhodobacter sphaeroides: protective role of carotenoids and expression of selected genes Microbiology 151 2005 1927 1938 (Pubitemid 40909035)
    • (2005) Microbiology , vol.151 , Issue.6 , pp. 1927-1938
    • Glaeser, J.1    Klug, G.2
  • 40
    • 4444313478 scopus 로고    scopus 로고
    • Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803
    • DOI 10.1021/bi036178q
    • Nishiyama Y., Allakhverdiev S.I., Yamamoto H., Hayashi H., and Murata N. Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803 Biochemistry 43 2004 11321 11330 (Pubitemid 39180376)
    • (2004) Biochemistry , vol.43 , Issue.35 , pp. 11321-11330
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Yamamoto, H.3    Hayashi, H.4    Murata, N.5
  • 41
    • 7744242257 scopus 로고    scopus 로고
    • Responses of the Rhodobacter sphaeroides transcriptome to blue light under semiaerobic conditions
    • DOI 10.1128/JB.186.22.7726-7735.2004
    • Braatsch S., Moskvin O.V., Klug G., and Gomelsky M. Responses of the Rhodobacter sphaeroides transcriptome to blue light under semiaerobic conditions J. Bacteriol. 186 2004 7726 7735 (Pubitemid 39463739)
    • (2004) Journal of Bacteriology , vol.186 , Issue.22 , pp. 7726-7735
    • Braatsch, S.1    Moskvin, O.V.2    Klug, G.3    Gomelsky, M.4
  • 43
    • 0033568606 scopus 로고    scopus 로고
    • The Escherichia coli σ(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ factor
    • DOI 10.1101/gad.13.18.2449
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor Genes Dev. 13 1999 2449 2461 (Pubitemid 29453615)
    • (1999) Genes and Development , vol.13 , Issue.18 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 44
    • 0344453810 scopus 로고    scopus 로고
    • E during initiation, adaptation, and shutoff of the extracytoplasmic heat shock response in Escherichia coli
    • DOI 10.1128/JB.185.8.2512-2519.2003
    • E during initiation, adaptation, and shutoff of the extracytoplasmic heat shock response in Escherichia coli J. Bacteriol. 185 2003 2512 2519 (Pubitemid 36417975)
    • (2003) Journal of Bacteriology , vol.185 , Issue.8 , pp. 2512-2519
    • Ades, S.E.1    Grigorova, I.L.2    Gross, C.A.3
  • 45
    • 2442563573 scopus 로고    scopus 로고
    • E-dependent envelope stress response
    • DOI 10.1111/j.1365-2958.2003.03982.x
    • E-dependent envelope stress response Mol. Microbiol. 52 2004 613 619 (Pubitemid 38621733)
    • (2004) Molecular Microbiology , vol.52 , Issue.3 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 46
    • 0346996698 scopus 로고    scopus 로고
    • Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: Zinc release and disulfide bond formation
    • Bae J.B., Park J.H., Hahn M.Y., Kim M.S., and Roe J.H. Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: zinc release and disulfide bond formation J. Mol. Biol. 335 2004 425 435
    • (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
  • 47
    • 33745865202 scopus 로고    scopus 로고
    • Zinc center as redox switch - New function for an old motif
    • DOI 10.1089/ars.2006.8.835
    • Ilbert M., Graf P.C., and Jakob U. Zinc center as redox switch-new function for an old motif Antioxid. Redox Signal. 8 2006 835 846 (Pubitemid 44036501)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.5-6 , pp. 835-846
    • Ilbert, M.1    Graf, P.C.F.2    Jakob, U.3
  • 49
    • 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 A.R., Bibb M.J., Buttner M.J., Paget M.S., and Kleanthous C. The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor J. Mol. Biol. 333 2003 461 472 (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
  • 50
    • 67349228432 scopus 로고    scopus 로고
    • Singlet-oxygen-mediated amino acid and protein oxidation: Formation of tryptophan peroxides and decomposition products
    • Gracanin M., Hawkins C.L., Pattison D.I., and Davies M.J. Singlet-oxygen-mediated amino acid and protein oxidation: formation of tryptophan peroxides and decomposition products Free Radical Biol. Med. 47 2009 92 102
    • (2009) Free Radical Biol. Med. , vol.47 , pp. 92-102
    • Gracanin, M.1    Hawkins, C.L.2    Pattison, D.I.3    Davies, M.J.4
  • 51
    • 67650543887 scopus 로고    scopus 로고
    • Severe zinc depletion of Escherichia coli: Roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins
    • Graham A.I., Hunt S., Stokes S.L., Bramall N., Bunch J., and Cox A.G. Severe zinc depletion of Escherichia coli: roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins J. Biol. Chem. 284 2009 18377 18389
    • (2009) J. Biol. Chem. , vol.284 , pp. 18377-18389
    • Graham, A.I.1    Hunt, S.2    Stokes, S.L.3    Bramall, N.4    Bunch, J.5    Cox, A.G.6
  • 54
    • 72849182812 scopus 로고
    • A requirement for sodium in the growth of Rhodopseudomonas spheroides
    • Sistrom W.R. A requirement for sodium in the growth of Rhodopseudomonas spheroides J. Gen. Microbiol. 22 1960 778 785
    • (1960) J. Gen. Microbiol. , vol.22 , pp. 778-785
    • Sistrom, W.R.1
  • 55
    • 0028934624 scopus 로고
    • ChrR positively regulates transcription of the Rhodobacter sphaeroides cytochrome c2 gene
    • Schilke B.A., and Donohue T.J. ChrR positively regulates transcription of the Rhodobacter sphaeroides cytochrome c2 gene J. Bacteriol. 177 1995 1929 1937
    • (1995) J. Bacteriol. , vol.177 , pp. 1929-1937
    • Schilke, B.A.1    Donohue, T.J.2
  • 56
    • 22544463928 scopus 로고    scopus 로고
    • Identification of genes required for recycling reducing power during photosynthetic growth
    • DOI 10.1128/JB.187.15.5249-5258.2005
    • Tavano C.L., Podevels A.M., and Donohue T.J. Identification of genes required for recycling reducing power during photosynthetic growth J. Bacteriol. 187 2005 5249 5258 (Pubitemid 41022944)
    • (2005) Journal of Bacteriology , vol.187 , Issue.15 , pp. 5249-5258
    • Tavano, C.L.1    Podevels, A.M.2    Donohue, T.J.3
  • 57
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT method
    • DOI 10.1006/meth.2001.1262
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(- Delta Delta C(T)) method Methods 25 2001 402 408 (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 58
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.