메뉴 건너뛰기




Volumn 154, Issue 7, 2008, Pages 1980-1988

Sulfur oxidation of Paracoccus pantotrophus: The sulfur-binding protein SoxYZ is the target of the periplasmic thiol-disulfide oxidoreductase SoxS

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL ANTIGEN; BINDING PROTEIN; CYSTEINE; PROTEIN ANTIBODY; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); SULFUR; SULFUR BINDING PROTEIN; THIOSULFATE;

EID: 51149102251     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2008/018655-0     Document Type: Article
Times cited : (15)

References (43)
  • 2
    • 0035184178 scopus 로고    scopus 로고
    • Identification of ccdA in Paracoccus pantotrophus GB17: Disruption of ccdA causes complete deficiency in c-type cytochromes
    • Bardischewsky, F. & Friedrich, C. G. (2001a). Identification of ccdA in Paracoccus pantotrophus GB17: disruption of ccdA causes complete deficiency in c-type cytochromes. J Bacteriol 183, 257-263.
    • (2001) J Bacteriol , vol.183 , pp. 257-263
    • Bardischewsky, F.1    Friedrich, C.G.2
  • 3
    • 0035928778 scopus 로고    scopus 로고
    • The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: A novel function in lithotrophy
    • Bardischewsky, F. & Friedrich, C. G. (2001b). The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: a novel function in lithotrophy. FEMS Microbiol Lett 202, 215-220.
    • (2001) FEMS Microbiol Lett , vol.202 , pp. 215-220
    • Bardischewsky, F.1    Friedrich, C.G.2
  • 4
    • 18244368975 scopus 로고    scopus 로고
    • Sulfur dehydrogenase of Paracoccus pantotrophus: The heme-2 domain of the molybdoprotein cytochrome c-complex is dispensable for catalytic activity
    • Bardischewsky, F., Quentmeier, A., Rother, D., Hellwig, P., Kostka, S, & Friedrich, C. G. (2005). Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c-complex is dispensable for catalytic activity. Biochemistry 44, 7024-7034.
    • (2005) Biochemistry , vol.44 , pp. 7024-7034
    • Bardischewsky, F.1    Quentmeier, A.2    Rother, D.3    Hellwig, P.4    Kostka, S.5    Friedrich, C.G.6
  • 5
    • 32244437878 scopus 로고    scopus 로고
    • SoxV transfers electrons to the periplasm of Paracoccus pantotrophus - an essential reaction for chemotrophic sulfur oxidation
    • Bardischewsky, F., Fischer, J., Höller, B. & Friedrich, C. G. (2006). SoxV transfers electrons to the periplasm of Paracoccus pantotrophus - an essential reaction for chemotrophic sulfur oxidation. Microbiology 152, 465-472.
    • (2006) Microbiology , vol.152 , pp. 465-472
    • Bardischewsky, F.1    Fischer, J.2    Höller, B.3    Friedrich, C.G.4
  • 6
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung, C. T., Niemela, S. L. & Miller, R. H. (1989). One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci U S A 86, 2172-2175.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 9
    • 0035408581 scopus 로고    scopus 로고
    • Oxidation of reduced inorganic sulfur compounds by bacteria: Emergence of a common mechanism?
    • Friedrich, C. G., Rother, D., Bardischewsky, F., Quentmeier, A. & Fischer, J. (2001). Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism? Appl Environ Microbiol 67, 2873-2882.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2873-2882
    • Friedrich, C.G.1    Rother, D.2    Bardischewsky, F.3    Quentmeier, A.4    Fischer, J.5
  • 11
    • 38849102092 scopus 로고    scopus 로고
    • Redox control of chemotrophic sulfur oxidation of Paracoccus pantotrophus
    • Edited by C. Dahl & C. G. Friedrich. Berlin: Springer Verlag
    • Friedrich,.C. G., Quentmeier, A, Bardischewsky, F., Rother, D., Orawski, G., Hellwig, P. & Fischer, J. (2008). Redox control of chemotrophic sulfur oxidation of Paracoccus pantotrophus. In Microbial Sulfur Metabolism, pp. 139-150. Edited by C. Dahl & C. G. Friedrich. Berlin: Springer Verlag.
    • (2008) Microbial Sulfur Metabolism , pp. 139-150
    • Friedrich, C.G.1    Quentmeier, A.2    Bardischewsky, F.3    Rother, D.4    Orawski, G.5    Hellwig, P.6    Fischer, J.7
  • 12
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura, H., Katzen, F. & Beckwith, J. (2003). Protein disulfide bond formation in prokaryotes. Annu Rev Biochem 72, 111-135.
    • (2003) Annu Rev Biochem , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 13
  • 14
    • 0021149499 scopus 로고
    • Factors affecting the isolation of CCC DNA from Streptomyces fividans and Escherichia coli
    • Kieser, T. (1984). Factors affecting the isolation of CCC DNA from Streptomyces fividans and Escherichia coli. Plasmid 12, 19-36.
    • (1984) Plasmid , vol.12 , pp. 19-36
    • Kieser, T.1
  • 15
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami, S., Kanaya, E, Kikuchi, M. & Ito, K. (1995). DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J Biol Chem 270, 17072-17074.
    • (1995) J Biol Chem , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 16
    • 0019904249 scopus 로고
    • Wide host range cloning vectors: A cosmid done bank of an Agrobacterium Ti plasmid
    • Knauf, V. C. & Nester, E. W. (1982). Wide host range cloning vectors: a cosmid done bank of an Agrobacterium Ti plasmid. Plasmid 8, 45-54.
    • (1982) Plasmid , vol.8 , pp. 45-54
    • Knauf, V.C.1    Nester, E.W.2
  • 17
    • 0021687639 scopus 로고
    • Different base/ base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coli
    • Kramer, B, Kramer, W. & Fritz, H. J. (1984). Different base/ base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coli. Cell 38, 879-887.
    • (1984) Cell , vol.38 , pp. 879-887
    • Kramer, B.1    Kramer, W.2    Fritz, H.J.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0042763566 scopus 로고    scopus 로고
    • Not every disulfide lasts forever: Disulfide bond formation as a redox switch
    • Linke, K. & Jakob, U. (2003). Not every disulfide lasts forever: disulfide bond formation as a redox switch. Antioxid Redox Signal 5, 425-434.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 425-434
    • Linke, K.1    Jakob, U.2
  • 20
    • 0027478696 scopus 로고
    • Transfer of Thiosphaera pantotropha to Paracoccus denitrificans
    • Ludwig, W., Mittenhuber, G. & Friedrich, C. G. (1993). Transfer of Thiosphaera pantotropha to Paracoccus denitrificans. Int J Syst Bacteriol 43, 363-367.
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 363-367
    • Ludwig, W.1    Mittenhuber, G.2    Friedrich, C.G.3
  • 21
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • Nakamoto, H. & dardwell, J. C. (2004). Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim Biophys Acta 1694, 111-119.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    dardwell, J.C.2
  • 22
    • 34247254977 scopus 로고    scopus 로고
    • The periplasmic thioredoxin SoxS plays a key role in activation in vivo of chemotrophic sulfur oxidation of Paracoccus pantotrophus
    • Orawski, G., Bardischewsky, F, Quentmeier, A., Rother, D. & Friedrich, C. G. (2007). The periplasmic thioredoxin SoxS plays a key role in activation in vivo of chemotrophic sulfur oxidation of Paracoccus pantotrophus. Microbiology 153, 1081-1086.
    • (2007) Microbiology , vol.153 , pp. 1081-1086
    • Orawski, G.1    Bardischewsky, F.2    Quentmeier, A.3    Rother, D.4    Friedrich, C.G.5
  • 24
    • 0035902915 scopus 로고    scopus 로고
    • The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB 17
    • Quentmeier, A. & Friedrich, C. G. (2001). The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB 17. FEBS Lett 503, 168-172.
    • (2001) FEBS Lett , vol.503 , pp. 168-172
    • Quentmeier, A.1    Friedrich, C.G.2
  • 25
    • 0344495378 scopus 로고    scopus 로고
    • Sulfur oxidation in Paracoccus pantotrophus: Interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB, protein
    • Quentmeier, A., Hellwig, P., Bardischewsky, F., Grelle, G., Kraft, R. & Friedrich, C. G. (2003). Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB, protein. Biochem Biophys Res Commun 312, 1011-1018.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 1011-1018
    • Quentmeier, A.1    Hellwig, P.2    Bardischewsky, F.3    Grelle, G.4    Kraft, R.5    Friedrich, C.G.6
  • 26
    • 34648827388 scopus 로고    scopus 로고
    • Activation of the heterodimeric central complex SoxYZ of chemotrophic sulfur oxidation is linked to a conformational change and SoxY-Y interprotein disulfide formation
    • Quentmeier, A., Janning, P., Hellwig, P. & Friedrich, C. G. (2007). Activation of the heterodimeric central complex SoxYZ of chemotrophic sulfur oxidation is linked to a conformational change and SoxY-Y interprotein disulfide formation. Biochemistry 46, 10990-10998.
    • (2007) Biochemistry , vol.46 , pp. 10990-10998
    • Quentmeier, A.1    Janning, P.2    Hellwig, P.3    Friedrich, C.G.4
  • 27
    • 0032943528 scopus 로고    scopus 로고
    • A re-evaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb. nov
    • Rainey, F. A., Kelly, D. P., Stackebrandt, E., Burghardt, J., Hiraishi, A., Katayama, Y. & Wood, A. P. (1999). A re-evaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb. nov. Int J Syst Bacteriol 49, 645-651.
    • (1999) Int J Syst Bacteriol , vol.49 , pp. 645-651
    • Rainey, F.A.1    Kelly, D.P.2    Stackebrandt, E.3    Burghardt, J.4    Hiraishi, A.5    Katayama, Y.6    Wood, A.P.7
  • 28
    • 0036125494 scopus 로고    scopus 로고
    • Redox state of cytoplasmic thioredoxin
    • Ritz, D. & Beckwith, J. (2002). Redox state of cytoplasmic thioredoxin. Methods Enzymol 347, 360-370.
    • (2002) Methods Enzymol , vol.347 , pp. 360-370
    • Ritz, D.1    Beckwith, J.2
  • 29
    • 0001328962 scopus 로고
    • Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultative autotrophic sulphur bacterium
    • Robertson, L. A. & Kuenen, J. G. (1983). Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultative autotrophic sulphur bacterium. J Gen Microbiol 129, 2847-2855.
    • (1983) J Gen Microbiol , vol.129 , pp. 2847-2855
    • Robertson, L.A.1    Kuenen, J.G.2
  • 30
    • 0034932333 scopus 로고    scopus 로고
    • Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur oxidizing system in Paracoccus pantotrophus GB17
    • Rother, D., Henrich, H.-J., Quentmeier, A., Bardischewsky, F. & Friedrich, C. G. (2001). Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur oxidizing system in Paracoccus pantotrophus GB17. J Bacteriol 183, 4499-4508.
    • (2001) J Bacteriol , vol.183 , pp. 4499-4508
    • Rother, D.1    Henrich, H.-J.2    Quentmeier, A.3    Bardischewsky, F.4    Friedrich, C.G.5
  • 31
    • 19044382770 scopus 로고    scopus 로고
    • SoxRS-mediated regulation of chemotrophic sulfur oxidation in Paracoccus pantotrophus
    • Rother,D., Orawski, G, Bardischewsky, F. & Friedrich, C. G. (2005). SoxRS-mediated regulation of chemotrophic sulfur oxidation in Paracoccus pantotrophus. Microbiology 151, 1707-1716.
    • (2005) Microbiology , vol.151 , pp. 1707-1716
    • Rother, D.1    Orawski, G.2    Bardischewsky, F.3    Friedrich, C.G.4
  • 33
  • 34
    • 34548183302 scopus 로고    scopus 로고
    • The SoxYZ complex carries sulfur cycle intermediates on a peptide swinging arm
    • Sauvé, V., Bruno, S., Berks, B. C. & Hemmings, A. M. (2007). The SoxYZ complex carries sulfur cycle intermediates on a peptide swinging arm. J Biol Chem 282, 23194-23204.
    • (2007) J Biol Chem , vol.282 , pp. 23194-23204
    • Sauvé, V.1    Bruno, S.2    Berks, B.C.3    Hemmings, A.M.4
  • 35
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., Priefer, U. & Pühler, A. (1983). A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1, 784-790.
    • (1983) Bio/Technology , vol.1 , pp. 784-790
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 36
    • 0000196317 scopus 로고
    • A colorimetric method for the determination of thiosulfate
    • Serbo, B. (1957). A colorimetric method for the determination of thiosulfate. Biochim Biophys Acta 23, 412-416.
    • (1957) Biochim Biophys Acta , vol.23 , pp. 412-416
    • Serbo, B.1
  • 37
    • 33947728050 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the sulfur carrier protein SoxY from Chlorobium limicola f. thiosulfatophilum reveals a tetrameric structure
    • Stout, J., Van Driessche, G., Savvides, S. N. & Van Beeumen, J. (2007). X-ray crystallographic analysis of the sulfur carrier protein SoxY from Chlorobium limicola f. thiosulfatophilum reveals a tetrameric structure. Protein Sci 16, 589-601.
    • (2007) Protein Sci , vol.16 , pp. 589-601
    • Stout, J.1    Van Driessche, G.2    Savvides, S.N.3    Van Beeumen, J.4
  • 38
    • 34249859204 scopus 로고    scopus 로고
    • Kinetic characterization of the disulfide bond-forming enzyme DsbB
    • Tapley, T. L., Eichner, T., Gleiter, S., Ballou, D. P. & Bardwell, J. C. A. (2007). Kinetic characterization of the disulfide bond-forming enzyme DsbB. J Biol Chem 282, 10263-10271.
    • (2007) J Biol Chem , vol.282 , pp. 10263-10271
    • Tapley, T.L.1    Eichner, T.2    Gleiter, S.3    Ballou, D.P.4    Bardwell, J.C.A.5
  • 39
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer, L. (1997). Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 61, 337-376.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Steehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76, 4350-4354.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Steehelin, T.2    Gordon, J.3
  • 41
    • 0015437962 scopus 로고
    • Measurement of molecular weights by electrophoresis on SDS polyacrylamide gel
    • Weber, K., Pringle, J. R. & Osborn, M. (1972). Measurement of molecular weights by electrophoresis on SDS polyacrylamide gel. Methods Enzymol 26, 3-27.
    • (1972) Methods Enzymol , vol.26 , pp. 3-27
    • Weber, K.1    Pringle, J.R.2    Osborn, M.3
  • 42
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 43
    • 0023359283 scopus 로고
    • DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residues
    • Zell, R. & Fritz, H. J. (1987). DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residues. EMBO J 6, 1809-1815.
    • (1987) EMBO J , vol.6 , pp. 1809-1815
    • Zell, R.1    Fritz, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.