메뉴 건너뛰기




Volumn 279, Issue 20, 2012, Pages 3828-3843

Functional and structural studies of the disulfide isomerase DsbC from the plant pathogen Xylella fastidiosa reveals a redox-dependent oligomeric modulation in vitro

Author keywords

biofilm formation; DsbC; oligomeric assembly; SAXS; Xylella fastidiosa

Indexed keywords

COPPER; PROTEIN DISULFIDE ISOMERASE; PROTEIN XFDSBC; UNCLASSIFIED DRUG;

EID: 84867099487     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08743.x     Document Type: Article
Times cited : (3)

References (65)
  • 1
    • 77950517981 scopus 로고    scopus 로고
    • Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA
    • Thakur KG, Praveena T, &, Gopal B, (2010) Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA. J Mol Biol 397, 1199-1208.
    • (2010) J Mol Biol , vol.397 , pp. 1199-1208
    • Thakur, K.G.1    Praveena, T.2    Gopal, B.3
  • 2
    • 84862548210 scopus 로고    scopus 로고
    • Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals
    • Sato Y, &, Inaba K, (2012) Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals. FEBS J 279, 2262-2271.
    • (2012) FEBS J , vol.279 , pp. 2262-2271
    • Sato, Y.1    Inaba, K.2
  • 3
    • 33645881071 scopus 로고    scopus 로고
    • Pathways of disulfide bond formation in Escherichia coli
    • Messens J, &, Collet JF, (2006) Pathways of disulfide bond formation in Escherichia coli. Int J Biochem Cell Biol 38, 1050-1062.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 1050-1062
    • Messens, J.1    Collet, J.F.2
  • 4
    • 41449093101 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Gleiter S, &, Bardwell JC, (2008) Disulfide bond isomerization in prokaryotes. Biochim Biophys Acta 1783, 530-534.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 530-534
    • Gleiter, S.1    Bardwell, J.C.2
  • 5
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura H, &, Beckwith J, (2010) Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal 13, 1231-1246.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1231-1246
    • Kadokura, H.1    Beckwith, J.2
  • 6
    • 78149469953 scopus 로고    scopus 로고
    • Multiple catalytically active thioredoxin folds: A winning strategy for many functions
    • Pedone E, Limauro D, D'Ambrosio K, De Simone G, &, Bartolucci S, (2010) Multiple catalytically active thioredoxin folds: a winning strategy for many functions. Cell Mol Life Sci 67, 3797-3814.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3797-3814
    • Pedone, E.1    Limauro, D.2    D'Ambrosio, K.3    De Simone, G.4    Bartolucci, S.5
  • 7
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich M, &, Glockshuber R, (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci 2, 717-726.
    • (1993) Protein Sci , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 8
    • 0032579404 scopus 로고    scopus 로고
    • Modeling charge interactions and redox properties in DsbA
    • Warwicker J, (1998) Modeling charge interactions and redox properties in DsbA. J Biol Chem 273, 2501-2504.
    • (1998) J Biol Chem , vol.273 , pp. 2501-2504
    • Warwicker, J.1
  • 9
    • 0033525640 scopus 로고    scopus 로고
    • Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
    • Hennecke J, Sebbel P, &, Glockshuber R, (1999) Random circular permutation of DsbA reveals segments that are essential for protein folding and stability. J Mol Biol 286, 1197-1215.
    • (1999) J Mol Biol , vol.286 , pp. 1197-1215
    • Hennecke, J.1    Sebbel, P.2    Glockshuber, R.3
  • 10
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch A, Belin D, Martin N, &, Beckwith J, (1996) An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc Natl Acad Sci USA 93, 13048-13053.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13048-13053
    • Rietsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 11
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker A, &, Bardwell JC, (2004) In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem 279, 12967-12973.
    • (2004) J Biol Chem , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.2
  • 13
    • 0035847099 scopus 로고    scopus 로고
    • Disulfide-dependent folding and export of Escherichia coli DsbC
    • Liu X, &, Wang CC, (2001) Disulfide-dependent folding and export of Escherichia coli DsbC. J Biol Chem 276, 1146-1151.
    • (2001) J Biol Chem , vol.276 , pp. 1146-1151
    • Liu, X.1    Wang, C.C.2
  • 15
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch A, Bessette P, Georgiou G, &, Beckwith J, (1997) Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol 179, 6602-6608.
    • (1997) J Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 19
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
    • Berkmen M, Boyd D, &, Beckwith J, (2005) The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J Biol Chem 280, 11387-11394.
    • (2005) J Biol Chem , vol.280 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 21
    • 26644437700 scopus 로고    scopus 로고
    • Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC
    • Hiniker A, Collet JF, &, Bardwell JC, (2005) Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J Biol Chem 280, 33785-33791.
    • (2005) J Biol Chem , vol.280 , pp. 33785-33791
    • Hiniker, A.1    Collet, J.F.2    Bardwell, J.C.3
  • 22
  • 23
    • 0027321646 scopus 로고
    • Culture and serological detection of the xylem-limited bacterium causing citrus variegated chlorosis and its identification as a strain of Xylella fastidiosa
    • Chang CJ, Garnier M, Zreik L, Rossetti V, &, Bové JM, (1993) Culture and serological detection of the xylem-limited bacterium causing citrus variegated chlorosis and its identification as a strain of Xylella fastidiosa. Curr Microbiol 27, 137-142.
    • (1993) Curr Microbiol , vol.27 , pp. 137-142
    • Chang, C.J.1    Garnier, M.2    Zreik, L.3    Rossetti, V.4    Bové, J.M.5
  • 24
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun A, Missiakas D, Raina S, &, Creighton TE, (1995) Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34, 5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 25
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
    • Fischer H, Neto MD, Napolitano HB, Polikarpov I, &, Craievich AF, (2010) Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale. J Appl Crystallogr 43, 101-109.
    • (2010) J Appl Crystallogr , vol.43 , pp. 101-109
    • Fischer, H.1    Neto, M.D.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 26
    • 69949177419 scopus 로고    scopus 로고
    • Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC
    • Arredondo SA, Chen TF, Riggs AF, Gilbert HF, &, Georgiou G, (2009) Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC. J Biol Chem 284, 23972-23979.
    • (2009) J Biol Chem , vol.284 , pp. 23972-23979
    • Arredondo, S.A.1    Chen, T.F.2    Riggs, A.F.3    Gilbert, H.F.4    Georgiou, G.5
  • 33
    • 84857127405 scopus 로고    scopus 로고
    • A novel protein refolding protocol for the solubilization and purification of recombinant peptidoglycan-associated lipoprotein from Xylella fastidiosa overexpressed in Escherichia coli
    • Santos CA, Beloti LL, Toledo MAS, Crucello A, Favaro MTP, Mendes JS, Santiago AS, Azzoni AR, &, Souza AP, (2012) A novel protein refolding protocol for the solubilization and purification of recombinant peptidoglycan-associated lipoprotein from Xylella fastidiosa overexpressed in Escherichia coli. Protein Expr Purif 82, 284-289.
    • (2012) Protein Expr Purif , vol.82 , pp. 284-289
    • Santos, C.A.1    Beloti, L.L.2    Toledo, M.A.S.3    Crucello, A.4    Favaro, M.T.P.5    Mendes, J.S.6    Santiago, A.S.7    Azzoni, A.R.8    Souza, A.P.9
  • 41
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, &, Hayer-Hartl M, (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 42
    • 33845585791 scopus 로고    scopus 로고
    • Folding of Escherichia coli DsbC: Characterization of a monomeric folding intermediate
    • Ke H, Zhang S, Li J, Howlett GJ, &, Wang CC, (2006) Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate. Biochemistry 45, 15100-15110.
    • (2006) Biochemistry , vol.45 , pp. 15100-15110
    • Ke, H.1    Zhang, S.2    Li, J.3    Howlett, G.J.4    Wang, C.C.5
  • 43
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, &, Ito K, (2006) Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127, 789-801.
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 45
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton RJ, Boyd D, Berkmen M, &, Beckwith J, (2008) Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc Natl Acad Sci USA 105, 11933-11938.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 46
    • 2642569160 scopus 로고    scopus 로고
    • Xylella fastidiosa subspecies: X. fastidiosa subsp. [correction] fastidiosa [correction] subsp. nov., X. fastidiosa subsp. multiplex subsp. nov. & X. fastidiosa subsp. pauca subsp. nov
    • Schaad NW, Postnikova E, Lacy G, Fatmi M, &, Chang CJ, (2004) Xylella fastidiosa subspecies: X. fastidiosa subsp. [correction] fastidiosa [correction] subsp. nov., X. fastidiosa subsp. multiplex subsp. nov. & X. fastidiosa subsp. pauca subsp. nov. Syst Appl Microbiol 27, 290-300.
    • (2004) Syst Appl Microbiol , vol.27 , pp. 290-300
    • Schaad, N.W.1    Postnikova, E.2    Lacy, G.3    Fatmi, M.4    Chang, C.J.5
  • 48
    • 34250247622 scopus 로고
    • Axenic culture of the bacteria associated with phony disease of peach and plum leaf scald
    • Davis MJ, French WJ, &, Schaad NW, (1981) Axenic culture of the bacteria associated with phony disease of peach and plum leaf scald. Curr Microbiol 5, 311-316.
    • (1981) Curr Microbiol , vol.5 , pp. 311-316
    • Davis, M.J.1    French, W.J.2    Schaad, N.W.3
  • 49
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL, (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82, 70-77.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 50
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A, (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254, 9627-9632.
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 51
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, Toyonaga H, &, Mori H, (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12, 291-299.
    • (2005) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 53
    • 0029018327 scopus 로고
    • Tight regulation, modulation & high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, &, Beckwith J, (1995) Tight regulation, modulation & high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177, 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 54
    • 43049164355 scopus 로고    scopus 로고
    • One-dimensional electrophoresis using nondenaturing conditions
    • Gallagher SR, (2001) One-dimensional electrophoresis using nondenaturing conditions. Curr Protoc Protein Sci 10, 10.3.1-10.3.11.
    • (2001) Curr Protoc Protein Sci , vol.10 , pp. 1031-10311
    • Gallagher, S.R.1
  • 55
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L, &, Wallace BA, (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32, W668-W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 57
    • 0029695129 scopus 로고    scopus 로고
    • Two-dimensional detector software: From real detector to idealised image or two-theta scan
    • Hammersley AP, Svensson SO, Hanfland M, Fitch AN, &, Hausermann D, (1996) Two-dimensional detector software: from real detector to idealised image or two-theta scan. High Press Res 14, 235-248.
    • (1996) High Press Res , vol.14 , pp. 235-248
    • Hammersley, A.P.1    Svensson, S.O.2    Hanfland, M.3    Fitch, A.N.4    Hausermann, D.5
  • 59
    • 0035354585 scopus 로고    scopus 로고
    • Changes in biomolecular conformation seen by small angle X-ray scattering
    • Doniach S, (2001) Changes in biomolecular conformation seen by small angle X-ray scattering. Chem Rev 101, 1763-1778.
    • (2001) Chem Rev , vol.101 , pp. 1763-1778
    • Doniach, S.1
  • 60
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke D, &, Svergun DI, (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J Appl Crystallogr 42, 342-346.
    • (2009) J Appl Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 61
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, &, Svergun DI, (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Crystallogr 36, 860-864.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 62
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, &, Zhang Y, (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5, 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 63
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, &, Svergun DI, (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89, 1237-1250.
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 64
    • 0029185933 scopus 로고
    • CRYSOL a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, &, Koch MHJ, (1995) CRYSOL a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28, 768-773.
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 65
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin MB, &, Svergun DI, (2001) Automated matching of high- and low-resolution structural models. J Appl Crystallogr 34, 33-41.
    • (2001) J Appl Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.