메뉴 건너뛰기




Volumn 81, Issue 2, 2012, Pages 193-200

Thermofluor-based optimization strategy for the stabilization and crystallization of Campylobacter jejuni desulforubrerythrin

Author keywords

Hydrogen peroxide; Metalloprotein; Oxidative stress; Rrc; Rubrerythrin

Indexed keywords

BACTERIAL PROTEIN; BUFFER; DESULFOREDOXIN; HEMERYTHRIN; IRON SULFUR PROTEIN; RECOMBINANT PROTEIN; RUBREDOXIN; RUBRERYTHRINS;

EID: 81155128023     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.10.001     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • E. Cabiscol, J. Tamarit, and J. Ros Oxidative stress in bacteria and protein damage by reactive oxygen species Int. Microbiol. 3 2000 3 8
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 2
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • S.B. Farr, and T. Kogoma Oxidative stress responses in Escherichia coli and Salmonella typhimurium Microbiol. Rev. 55 1991 561 585 (Pubitemid 21895167)
    • (1991) Microbiological Reviews , vol.55 , Issue.4 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 3
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • DOI 10.1006/abbi.1999.1518
    • D. Touati Iron and oxidative stress in bacteria Arch. Biochem. Biophys. 373 2000 1 6 (Pubitemid 30046483)
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.1 , pp. 1-6
    • Touati, D.1
  • 4
    • 0001845568 scopus 로고    scopus 로고
    • Molecular mechanisms of oxidative stress in aging: Free radicals, aging, antioxidants and disease
    • M. Pollack, and C. Leeuwenburgh Molecular mechanisms of oxidative stress in aging: free radicals, aging, antioxidants and disease Elsevier Science 30 1999 881 923
    • (1999) Elsevier Science , vol.30 , pp. 881-923
    • Pollack, M.1    Leeuwenburgh, C.2
  • 5
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • DOI 10.1038/nrm2256, PII NRM2256
    • B. D'Autreaux, and M.B. Toledano ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis Nat. Rev. Mol. Cell Biol. 8 2007 813 824 (Pubitemid 47462134)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 6
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of Oxidative Damage
    • DOI 10.1146/annurev.micro.57.030502.090938
    • J.A. Imlay Pathways of oxidative damage Annu. Rev. Microbiol. 57 2003 395 418 (Pubitemid 37392949)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 8
    • 74449083884 scopus 로고    scopus 로고
    • Reductive elimination of superoxide: Structure and mechanism of superoxide reductases
    • A.F. Pinto, J.V. Rodrigues, and M. Teixeira Reductive elimination of superoxide: structure and mechanism of superoxide reductases Biochim. Biophys. Acta 1804 2010 285 297
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 285-297
    • Pinto, A.F.1    Rodrigues, J.V.2    Teixeira, M.3
  • 10
    • 77953807027 scopus 로고    scopus 로고
    • The ferritin-like superfamily: Evolution of the biological iron storeman from a rubrerythrin-like ancestor
    • S.C. Andrews The ferritin-like superfamily: evolution of the biological iron storeman from a rubrerythrin-like ancestor Biochim. Biophys. Acta 1800 2010 691 705
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 691-705
    • Andrews, S.C.1
  • 11
    • 0035476428 scopus 로고    scopus 로고
    • A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: Catalytic electron transfer to rubrerythrin and two-iron superoxide reductase
    • DOI 10.1006/abbi.2001.2531
    • E.D. Coulter, and D.M. Kurtz Jr. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase Arch Biochem. Biophys. 394 2001 76 86 (Pubitemid 32948287)
    • (2001) Archives of Biochemistry and Biophysics , vol.394 , Issue.1 , pp. 76-86
    • Coulter, E.D.1    Kurtz Jr., D.M.2
  • 12
    • 0035190269 scopus 로고    scopus 로고
    • Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: A novel oxidative stress protection system
    • DOI 10.1128/JB.183.1.101-108.2001
    • H.L. Lumppio, N.V. Shenvi, A.O. Summers, G. Voordouw, and D.M. Kurtz Jr. Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system J. Bacteriol. 183 2001 101 108 (Pubitemid 32003113)
    • (2001) Journal of Bacteriology , vol.183 , Issue.1 , pp. 101-108
    • Lumppio, H.L.1    Shenvi, N.V.2    Summers, A.O.3    Voordouw, G.4    Kurtz Jr., D.M.5
  • 13
    • 0035119328 scopus 로고    scopus 로고
    • Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin
    • DOI 10.1128/JB.183.5.1560-1567.2001
    • A. Das, E.D. Coulter, D.M. Kurtz Jr., and L.G. Ljungdahl Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein-high-molecular-weight rubredoxin J. Bacteriol. 183 2001 1560 1567 (Pubitemid 32172298)
    • (2001) Journal of Bacteriology , vol.183 , Issue.5 , pp. 1560-1567
    • Das, A.1    Coulter, E.D.2    Kurtz Jr., D.M.3    Ljungdahl, L.G.4
  • 14
    • 57749205262 scopus 로고    scopus 로고
    • Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum
    • O. Riebe, R.J. Fischer, D.A. Wampler, D.M. Kurtz Jr., and H. Bahl Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum Microbiology 155 2009 16 24
    • (2009) Microbiology , vol.155 , pp. 16-24
    • Riebe, O.1    Fischer, R.J.2    Wampler, D.A.3    Kurtz, Jr.D.M.4    Bahl, H.5
  • 17
    • 0038182901 scopus 로고    scopus 로고
    • EPR and ENDOR evidence for a 1-His, hydroxo-bridged mixed-valent diiron site in Desulfovibrio vulgaris rubrerythrin
    • DOI 10.1021/bi0300027
    • S.K. Smoukov, R.M. Davydov, P.E. Doan, B. Sturgeon, I.Y. Kung, B.M. Hoffman, and D.M. Kurtz Jr. EPR and ENDOR evidence for a 1-His, hydroxo-bridged mixed-valent diiron site in Desulfovibrio vulgaris rubrerythrin Biochemistry 42 2003 6201 6208 (Pubitemid 36605122)
    • (2003) Biochemistry , vol.42 , Issue.20 , pp. 6201-6208
    • Smoukov, S.K.1    Davydov, R.M.2    Doan, P.E.3    Sturgeon, B.4    Kung, I.Y.5    Hoffman, B.M.6    Kurtz Jr., D.M.7
  • 18
    • 0036229440 scopus 로고    scopus 로고
    • Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis
    • DOI 10.1046/j.1365-2958.2002.02892.x
    • M. Sztukowska, M. Bugno, J. Potempa, J. Travis, and D.M. Kurtz Jr. Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis Mol Microbiol 44 2002 479 488 (Pubitemid 34429749)
    • (2002) Molecular Microbiology , vol.44 , Issue.2 , pp. 479-488
    • Sztukowska, M.1    Bugno, M.2    Potempa, J.3    Travis, J.4    Kurtz Jr., D.M.5
  • 19
    • 0024281294 scopus 로고
    • Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster
    • J. LeGall, B.C. Prickril, I. Moura, A.V. Xavier, J.J.G. Moura, and H.B. Hanh Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster Biochemistry 27 1988 1636 1642
    • (1988) Biochemistry , vol.27 , pp. 1636-1642
    • Legall, J.1    Prickril, B.C.2    Moura, I.3    Xavier, A.V.4    Moura, J.J.G.5    Hanh, H.B.6
  • 20
    • 0030474295 scopus 로고    scopus 로고
    • Rubrerythrin from Clostridium perfringens: Cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function
    • Y. Lehmann, L. Meile, and M. Teuber Rubrerythrin from Clostridium perfringens: cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function J. Bacteriol. 178 1996 7152 7158 (Pubitemid 26424628)
    • (1996) Journal of Bacteriology , vol.178 , Issue.24 , pp. 7152-7158
    • Lehmann, Y.1    Meile, L.2    Teuber, M.3
  • 21
    • 0141954187 scopus 로고    scopus 로고
    • Crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping
    • DOI 10.1021/bi034220b
    • S. Fushinobu, H. Shoun, and T. Wakagi Crystal structure of sulerythrin, a rubrerythrin-like protein from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7, shows unexpected domain swapping Biochemistry 42 2003 11707 11715 (Pubitemid 37243631)
    • (2003) Biochemistry , vol.42 , Issue.40 , pp. 11707-11715
    • Fushinobu, S.1    Shoun, H.2    Wakagi, T.3
  • 22
    • 20644461004 scopus 로고    scopus 로고
    • Rubrerythrin and peroxiredoxin: Two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis
    • DOI 10.1016/j.molbiopara.2005.04.003, PII S0166685105001337
    • S. Pütz, G. Gelius-Dietrich, M. Piotrowski, and K. Henze Rubrerythrin and peroxiredoxin: two novel putative peroxidases in the hydrogenosomes of the microaerophilic protozoon Trichomonas vaginalis Mol. Biochem. Parasitol. 142 2005 212 223 (Pubitemid 40835913)
    • (2005) Molecular and Biochemical Parasitology , vol.142 , Issue.2 , pp. 212-223
    • Putz, S.1    Gelius-Dietrich, G.2    Piotrowski, M.3    Henze, K.4
  • 24
    • 0025786652 scopus 로고
    • The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: Comparison with hemerythrin and rubredoxin
    • J.J. Van Beeumen, G. Van Driessche, M.Y. Liu, and J. LeGall The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with hemerythrin and rubredoxin J. Biol. Chem. 266 1991 20645 20653 (Pubitemid 21908511)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.31 , pp. 20645-20653
    • Van Beeument, J.J.1    Van Driessche, G.2    Liu, M.-Y.3    LeGall, J.4
  • 26
    • 2442665515 scopus 로고    scopus 로고
    • Identification of an oxidative stress-sensitive protein from Campylobacter jejuni, homologous to rubredoxin oxidoreductase/rubrerythrin
    • DOI 10.1016/j.femsle.2004.04.012, PII S037810970400271X
    • M. Yamasaki, S. Igimi, Y. Katayama, S. Yamamoto, and F. Amano Identification of an oxidative stress-sensitive protein from Campylobacter jejuni, homologous to rubredoxin oxidoreductase/rubrerythrin FEMS Microbiol. Lett. 235 2004 57 63 (Pubitemid 38668637)
    • (2004) FEMS Microbiology Letters , vol.235 , Issue.1 , pp. 57-63
    • Yamasaki, M.1    Igimi, S.2    Katayama, Y.3    Yamamoto, S.4    Amano, F.5
  • 27
    • 79960001045 scopus 로고    scopus 로고
    • Comparison of fluorescence and light scattering based methods to assess formation and stability of protein-protein complexes
    • J. Kopec, and G. Schneider Comparison of fluorescence and light scattering based methods to assess formation and stability of protein-protein complexes J. Struct. Biol. 175 2011 216 223
    • (2011) J. Struct. Biol. , vol.175 , pp. 216-223
    • Kopec, J.1    Schneider, G.2
  • 28
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • M.R. Eftink The use of fluorescence methods to monitor unfolding transitions in proteins Biophys. J. 66 1994 482 501 (Pubitemid 24058467)
    • (1994) Biophysical Journal , vol.66 , Issue.2 , pp. 482-501
    • Eftink, M.R.1
  • 30
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • DOI 10.1021/bi00481a024
    • J.F. Brandts, and L.N. Lin Study of strong to ultratight protein interactions using differential scanning calorimetry Biochemistry 29 1990 6927 6940 (Pubitemid 20225495)
    • (1990) Biochemistry , vol.29 , Issue.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.-N.2
  • 31
    • 11844304103 scopus 로고    scopus 로고
    • Measurement of protein stability and protein denaturation in cells using differential scanning calorimetry
    • DOI 10.1016/j.ymeth.2004.08.002, PII S104620230400177X
    • J.R. Lepock Measurement of protein stability and protein denaturation in cells using differential scanning calorimetry Methods 35 2005 117 125 (Pubitemid 40092637)
    • (2005) Methods , vol.35 , Issue.2 , pp. 117-125
    • Lepock, J.R.1
  • 32
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • DOI 10.1016/j.ab.2006.07.027, PII S0003269706005355
    • U.B. Ericsson, B.M. Hallberg, G.T. Detitta, N. Dekker, and P. Nordlund Thermofluor-based high-throughput stability optimization of proteins for structural studies Anal. Biochem. 357 2006 289 298 (Pubitemid 44430091)
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 33
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using thermofluor
    • DOI 10.1021/bi048135v
    • D. Matulis, J.K. Kranz, F.R. Salemme, and M.J. Todd Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using thermofluor Biochemistry 44 2005 5258 5266 (Pubitemid 40471238)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 34
    • 43049095602 scopus 로고    scopus 로고
    • Methods for protein characterization by mass spectrometry, thermal shift (thermofluor) assay, and multiangle or static light scattering
    • J.E. Nettleship, J. Brown, M.R. Groves, and A. Geerlof Methods for protein characterization by mass spectrometry, thermal shift (thermofluor) assay, and multiangle or static light scattering Methods Mol. Biol. 426 2008 299 318
    • (2008) Methods Mol. Biol. , vol.426 , pp. 299-318
    • Nettleship, J.E.1    Brown, J.2    Groves, M.R.3    Geerlof, A.4
  • 35
    • 33749850046 scopus 로고    scopus 로고
    • Universal screening methods and applications of ThermoFluor®
    • DOI 10.1177/1087057106292746
    • M.D. Cummings, M.A. Farnum, and M.I. Nelen Universal screening methods and applications of thermofluor J. Biomol. Screen. 11 2006 854 863 (Pubitemid 44562327)
    • (2006) Journal of Biomolecular Screening , vol.11 , Issue.7 , pp. 854-863
    • Cummings, M.D.1    Farnum, M.A.2    Nelen, M.I.3
  • 38
    • 84859470677 scopus 로고    scopus 로고
    • < http://www.neb.com/nebecomm/products/productE8000.asp >.
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0029949340 scopus 로고    scopus 로고
    • 4 and ferritin-like diiron domains
    • DOI 10.1038/nsb0696-539
    • F. deMaré, D.M. Kurtz Jr., and P. Nordlund The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains Nat. Struct. Biol. 3 1996 539 546 (Pubitemid 26174703)
    • (1996) Nature Structural Biology , vol.3 , Issue.6 , pp. 539-546
    • DeMare, F.1    Kurtz Jr., D.M.2    Nordlund, P.3
  • 42
    • 0029123025 scopus 로고
    • Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 resolution: A novel non-heme iron protein structure
    • M. Archer, R. Huber, P. Tavares, I. Moura, J.J. Moura, M.A. Carrondo, L.C. Sieker, J. LeGall, and M.J. Romao Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 resolution: a novel non-heme iron protein structure J. Mol. Biol. 251 1995 690 702
    • (1995) J. Mol. Biol. , vol.251 , pp. 690-702
    • Archer, M.1    Huber, R.2    Tavares, P.3    Moura, I.4    Moura, J.J.5    Carrondo, M.A.6    Sieker, L.C.7    Legall, J.8    Romao, M.J.9
  • 44
    • 5044250423 scopus 로고    scopus 로고
    • Protein isoelectric point as a predictor for increased crystallization screening efficiency
    • DOI 10.1093/bioinformatics/bth066
    • K.A. Kantardjieff, and B. Rupp Protein isoelectric point as a predictor for increased crystallization screening efficiency Bioinformatics 20 2004 2162 2168 (Pubitemid 39341602)
    • (2004) Bioinformatics , vol.20 , Issue.14 , pp. 2162-2168
    • Kantardjieff, K.A.1    Rupp, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.