메뉴 건너뛰기




Volumn 77, Issue 5, 2010, Pages 1111-1122

SurR regulates hydrogen production in Pyrococcus furiosus by a sulfur-dependent redox switch

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; HYDROGENASE; PROTEIN SURR; SULFUR; UNCLASSIFIED DRUG;

EID: 77956136587     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07275.x     Document Type: Article
Times cited : (36)

References (56)
  • 1
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: Transcription regulation and beyond
    • Aravind, L., Anantharaman, V., Balaji, S., Babu, M.M. Iyer, L.M. (2005) The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol Rev 29 : 231 262.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 231-262
    • Aravind, L.1    Anantharaman, V.2    Balaji, S.3    Babu, M.M.4    Iyer, L.M.5
  • 2
    • 27844564819 scopus 로고    scopus 로고
    • Determinants of transcription initiation by archaeal RNA polymerase
    • Bartlett, M.S. (2005) Determinants of transcription initiation by archaeal RNA polymerase. Curr Opin Microbiol 8 : 677 684.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 677-684
    • Bartlett, M.S.1
  • 3
    • 20344396840 scopus 로고    scopus 로고
    • Archaeal transcriptional regulation - Variation on a bacterial theme?
    • Bell, S.D. (2005) Archaeal transcriptional regulation - variation on a bacterial theme? Trends Microbiol 13 : 262 265.
    • (2005) Trends Microbiol , vol.13 , pp. 262-265
    • Bell, S.D.1
  • 4
    • 0033400812 scopus 로고    scopus 로고
    • Transcriptional regulation of an archaeal operon in vivo and in vitro
    • Bell, S.D., Cairns, S.S., Robson, R.L. Jackson, S.P. (1999) Transcriptional regulation of an archaeal operon in vivo and in vitro. Mol Cell 4 : 971 982.
    • (1999) Mol Cell , vol.4 , pp. 971-982
    • Bell, S.D.1    Cairns, S.S.2    Robson, R.L.3    Jackson, S.P.4
  • 5
    • 0025236474 scopus 로고
    • Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Blumentals, I.I., Itoh, M., Olson, G.J. Kelly, R.M. (1990) Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl Environ Microbiol 56 : 1255 1262.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1255-1262
    • Blumentals, I.I.1    Itoh, M.2    Olson, G.J.3    Kelly, R.M.4
  • 6
    • 0037119358 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability
    • Brinkman, A.B., Bell, S.D., Lebbink, R.J., de Vos, W.M. van der Oost, J. (2002) The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability. J Biol Chem 277 : 29537 29549.
    • (2002) J Biol Chem , vol.277 , pp. 29537-29549
    • Brinkman, A.B.1    Bell, S.D.2    Lebbink, R.J.3    De Vos, W.M.4    Van Der Oost, J.5
  • 7
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner, L.S., Pennella, M.A. Giedroc, D.P. (2003) The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol Rev 27 : 131 143.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 8
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi, H., Kim, S., Mukhopadhyay, P., Cho, S., Woo, J., Storz, G. Ryu, S. (2001) Structural basis of the redox switch in the OxyR transcription factor. Cell 105 : 103 113.
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.7
  • 9
    • 35248900501 scopus 로고    scopus 로고
    • Hydrogen bonds in protein-DNA complexes: Where geometry meets plasticity
    • Coulocheri, S.A., Pigis, D.G., Papavassiliou, K.A. Papavassiliou, A.G. (2007) Hydrogen bonds in protein-DNA complexes: where geometry meets plasticity. Biochimie 89 : 1291 1303.
    • (2007) Biochimie , vol.89 , pp. 1291-1303
    • Coulocheri, S.A.1    Pigis, D.G.2    Papavassiliou, K.A.3    Papavassiliou, A.G.4
  • 10
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan, K.D. Zhang, K.Y. (1999) Density modification for macromolecular phase improvement. Prog Biophys Mol Biol 72 : 245 270.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 11
    • 77956147017 scopus 로고    scopus 로고
    • Modification of Cysteine
    • Coligan, J.E. ed.). Brooklyn, NY. Wiley
    • Crankshaw, M.W. Grant, G.A. (1996) Modification of Cysteine. In Current Protocols in Protein Science. Coligan, J.E. (ed.). Brooklyn, NY : Wiley, pp. 15.1.1 15.1.16.
    • (1996) Current Protocols in Protein Science , pp. 1511-15116
    • Crankshaw, M.W.1    Grant, G.A.2
  • 12
    • 0030565935 scopus 로고    scopus 로고
    • A novel approach to crystallising proteins under oil
    • Darcy, A., Elmore, C., Stihle, M. Johnston, J.E. (1996) A novel approach to crystallising proteins under oil. J Cryst Growth 168 : 175 180.
    • (1996) J Cryst Growth , vol.168 , pp. 175-180
    • Darcy, A.1    Elmore, C.2    Stihle, M.3    Johnston, J.E.4
  • 13
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution
    • Declercq, J.P., Evrard, C., Clippe, A., Stricht, D.V., Bernard, A. Knoops, B. (2001) Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. J Mol Biol 311 : 751 759.
    • (2001) J Mol Biol , vol.311 , pp. 751-759
    • Declercq, J.P.1    Evrard, C.2    Clippe, A.3    Stricht, D.V.4    Bernard, A.5    Knoops, B.6
  • 14
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 : 2126 2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 15
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100-degrees C
    • Fiala, G. Stetter, K.O. (1986) Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100-degrees C. Arch Microbiol 145 : 56 61.
    • (1986) Arch Microbiol , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 16
    • 0141679346 scopus 로고    scopus 로고
    • Identity and functions of CxxC-derived motifs
    • Fomenko, D.E. Gladyshev, V.N. (2003) Identity and functions of CxxC-derived motifs. Biochemistry 42 : 11214 11225.
    • (2003) Biochemistry , vol.42 , pp. 11214-11225
    • Fomenko, D.E.1    Gladyshev, V.N.2
  • 17
    • 0018199224 scopus 로고
    • DNAse footprinting: A simple method for the detection of protein-DNA binding specificity
    • Galas, D.J. Schmitz, A. (1978) DNAse footprinting: a simple method for the detection of protein-DNA binding specificity. Nucleic Acids Res 5 : 3157 3170.
    • (1978) Nucleic Acids Res , vol.5 , pp. 3157-3170
    • Galas, D.J.1    Schmitz, A.2
  • 18
    • 20344386725 scopus 로고    scopus 로고
    • Archaeal transcription and its regulators
    • Geiduschek, E.P. Ouhammouch, M. (2005) Archaeal transcription and its regulators. Mol Microbiol 56 : 1397 1407.
    • (2005) Mol Microbiol , vol.56 , pp. 1397-1407
    • Geiduschek, E.P.1    Ouhammouch, M.2
  • 19
  • 21
    • 0029906412 scopus 로고    scopus 로고
    • A cell-free transcription system for the hyperthermophilic archaeon Pyrococcus furiosus
    • Hethke, C., Geerling, A.C., Hausner, W., de Vos, W.M. Thomm, M. (1996) A cell-free transcription system for the hyperthermophilic archaeon Pyrococcus furiosus. Nucleic Acids Res 24 : 2369 2376.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2369-2376
    • Hethke, C.1    Geerling, A.C.2    Hausner, W.3    De Vos, W.M.4    Thomm, M.5
  • 22
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm, L. Park, J. (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16 : 566 567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 23
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L. Sander, C. (1996) Mapping the protein universe. Science 273 : 595 603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 27
    • 26444589081 scopus 로고    scopus 로고
    • Kinetics of the chemical oxidation of polysulfide anions in aqueous solution
    • Kleinjan, W.E., de Keizer, A. Janssen, A.J. (2005) Kinetics of the chemical oxidation of polysulfide anions in aqueous solution. Water Res 39 : 4093 4100.
    • (2005) Water Res , vol.39 , pp. 4093-4100
    • Kleinjan, W.E.1    De Keizer, A.2    Janssen, A.J.3
  • 28
    • 57149085868 scopus 로고    scopus 로고
    • Genomics of bacteria and archaea: The emerging dynamic view of the prokaryotic world
    • Koonin, E.V. Wolf, Y.I. (2008) Genomics of bacteria and archaea: the emerging dynamic view of the prokaryotic world. Nucleic Acids Res 36 : 6688 6719.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6688-6719
    • Koonin, E.V.1    Wolf, Y.I.2
  • 29
    • 0029006990 scopus 로고
    • Diamide: An oxidant probe for thiols
    • Kosower, N.S. Kosower, E.M. (1995) Diamide: an oxidant probe for thiols. Methods Enzymol 251 : 123 133.
    • (1995) Methods Enzymol , vol.251 , pp. 123-133
    • Kosower, N.S.1    Kosower, E.M.2
  • 30
    • 0037428467 scopus 로고    scopus 로고
    • TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis
    • Lee, S.J., Engelmann, A., Horlacher, R., Qu, Q., Vierke, G., Hebbeln, C., et al. (2003) TrmB, a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter from the hyperthermophilic archaeon Thermococcus litoralis. J Biol Chem 278 : 983 990.
    • (2003) J Biol Chem , vol.278 , pp. 983-990
    • Lee, S.J.1    Engelmann, A.2    Horlacher, R.3    Qu, Q.4    Vierke, G.5    Hebbeln, C.6
  • 31
    • 25144461083 scopus 로고    scopus 로고
    • TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers
    • Lee, S.J., Moulakakis, C., Koning, S.M., Hausner, W., Thomm, M. Boos, W. (2005) TrmB, a sugar sensing regulator of ABC transporter genes in Pyrococcus furiosus exhibits dual promoter specificity and is controlled by different inducers. Mol Micro 57 : 1797 1807.
    • (2005) Mol Micro , vol.57 , pp. 1797-1807
    • Lee, S.J.1    Moulakakis, C.2    Koning, S.M.3    Hausner, W.4    Thomm, M.5    Boos, W.6
  • 32
    • 14044255851 scopus 로고    scopus 로고
    • Regulation of nif expression in Methanococcus maripaludis- roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators
    • Lie, T.J., Wood, G.E. Leigh, J.A. (2005) Regulation of nif expression in Methanococcus maripaludis- roles of the euryarchaeal repressor NrpR, 2-oxoglutarate, and two operators. J Biol Chem 280 : 5236 5241.
    • (2005) J Biol Chem , vol.280 , pp. 5236-5241
    • Lie, T.J.1    Wood, G.E.2    Leigh, J.A.3
  • 33
    • 58149301541 scopus 로고    scopus 로고
    • SurR: A transcriptional activator and repressor controlling hydrogen and elemental sulphur metabolism in Pyrococcus furiosus
    • Lipscomb, G.L., Keese, A.M., Cowart, D.M., Schut, G.J., Thomm, M., Adams, M.W. Scott, R.A. (2009) SurR: a transcriptional activator and repressor controlling hydrogen and elemental sulphur metabolism in Pyrococcus furiosus. Mol Microbiol 71 : 332 349.
    • (2009) Mol Microbiol , vol.71 , pp. 332-349
    • Lipscomb, G.L.1    Keese, A.M.2    Cowart, D.M.3    Schut, G.J.4    Thomm, M.5    Adams, M.W.6    Scott, R.A.7
  • 34
    • 34247580135 scopus 로고    scopus 로고
    • Crystal structure of the archaeal heat shock regulator from Pyrococcus furiosus: A molecular chimera representing eukaryal and bacterial features
    • Liu, W., Vierke, G., Wenke, A.K., Thomm, M. Ladenstein, R. (2007) Crystal structure of the archaeal heat shock regulator from Pyrococcus furiosus: a molecular chimera representing eukaryal and bacterial features. J Mol Biol 369 : 474 488.
    • (2007) J Mol Biol , vol.369 , pp. 474-488
    • Liu, W.1    Vierke, G.2    Wenke, A.K.3    Thomm, M.4    Ladenstein, R.5
  • 37
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A.J. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63 : 32 41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 38
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej, T., Gibrat, J.F. Bryant, S.H. (1995) Threading a database of protein cores. Proteins 23 : 356 369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.F.2    Bryant, S.H.3
  • 40
    • 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. (2005) Redox-sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx. Mol Microbiol 55 : 498 510.
    • (2005) Mol Microbiol , vol.55 , pp. 498-510
    • Nakano, S.1    Erwin, K.N.2    Ralle, M.3    Zuber, P.4
  • 41
    • 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
    • Newberry, K.J., Nakano, S., Zuber, P. Brennan, R.G. (2005) 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 USA 102 : 15839 15844.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15839-15844
    • Newberry, K.J.1    Nakano, S.2    Zuber, P.3    Brennan, R.G.4
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276 : 307 326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget, M.S. Buttner, M.J. (2003) Thiol-based regulatory switches. Annu Rev Genet 37 : 91 121.
    • (2003) Annu Rev Genet , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 44
    • 4344586909 scopus 로고    scopus 로고
    • Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A member of a novel protein family related to protein disulfide-isomerase
    • Pedone, E., Ren, B., Ladenstein, R., Rossi, M. Bartolucci, S. (2004) Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: a member of a novel protein family related to protein disulfide-isomerase. Eur J Biochem 271 : 3437 3448.
    • (2004) Eur J Biochem , vol.271 , pp. 3437-3448
    • Pedone, E.1    Ren, B.2    Ladenstein, R.3    Rossi, M.4    Bartolucci, S.5
  • 45
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. Lamzin, V.S. (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6 : 458 463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 47
    • 0031816805 scopus 로고    scopus 로고
    • A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
    • Ren, B., Tibbelin, G., de Pascale, D., Rossi, M., Bartolucci, S. Ladenstein, R. (1998) A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units. Nat Struct Biol 5 : 602 611.
    • (1998) Nat Struct Biol , vol.5 , pp. 602-611
    • Ren, B.1    Tibbelin, G.2    De Pascale, D.3    Rossi, M.4    Bartolucci, S.5    Ladenstein, R.6
  • 48
    • 34250336912 scopus 로고    scopus 로고
    • Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: Characterization of a coenzyme A- dependent NAD(P)H sulfur oxidoreductase
    • Schut, G.J., Bridger, S.L. Adams, M.W. (2007) Insights into the metabolism of elemental sulfur by the hyperthermophilic archaeon Pyrococcus furiosus: characterization of a coenzyme A- dependent NAD(P)H sulfur oxidoreductase. J Bacteriol 189 : 4431 4441.
    • (2007) J Bacteriol , vol.189 , pp. 4431-4441
    • Schut, G.J.1    Bridger, S.L.2    Adams, M.W.3
  • 49
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • Storz, G., Tartaglia, L.A. Ames, B.N. (1990) Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248 : 189 194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 50
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41 : 207 234.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 52
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger, T.C. (2002) Automated structure solution, density modification and model building. Acta Crystallogr D Biol Crystallogr 58 : 1937 1940.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 : 4673 4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 55
    • 0037414803 scopus 로고    scopus 로고
    • A novel archaeal transcriptional regulator of heat shock response
    • Vierke, G., Engelmann, A., Hebbeln, C. Thomm, M. (2003) A novel archaeal transcriptional regulator of heat shock response. J Biol Chem 278 : 18 26.
    • (2003) J Biol Chem , vol.278 , pp. 18-26
    • Vierke, G.1    Engelmann, A.2    Hebbeln, C.3    Thomm, M.4
  • 56
    • 0034935287 scopus 로고    scopus 로고
    • Nonradiochemical DNase i footprinting by capillary electrophoresis
    • Wilson, D.O., Johnson, P. McCord, B.R. (2001) Nonradiochemical DNase I footprinting by capillary electrophoresis. Electrophoresis 22 : 1979 1986.
    • (2001) Electrophoresis , vol.22 , pp. 1979-1986
    • Wilson, D.O.1    Johnson, P.2    McCord, B.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.