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Applied and Environmental Microbiology
Volumn 80, Issue 7, 2014, Pages 2279-2292
A comparative quantitative proteomic study identifies new proteins relevant for sulfur oxidation in the purple sulfur bacterium allochromatium vinosum
Author keywords

[No Author keywords available]
Indexed keywords

GENES; METABOLISM; OXIDATION; PHYSIOLOGY; SULFUR;
EID: 84896041398     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.04182-13     Document Type: Article
Times cited : (38)
References (71)
  • 1
    • 84874946313 scopus 로고    scopus 로고
    • 15 December. eLS. John Wiley & Sons, Ltd, Chichester, United Kingdom
    • Dahl C, Friedrich CG, Kletzin A. 15 December 2008. Sulfur oxidation in prokaryotes. In eLS. John Wiley & Sons, Ltd, Chichester, United Kingdom. http://dx.doi.org/10.1002/9780470015902.a0021155.
    • (2008) Sulfur oxidation in prokaryotes
    • Dahl, C.1    Friedrich, C.G.2    Kletzin, A.3
  • 2
    • 52949095063 scopus 로고    scopus 로고
    • Sulfur metabolism in phototrophic sulfur bacteria
    • Frigaard N-U, Dahl C. 2009. Sulfur metabolism in phototrophic sulfur bacteria. Adv. Microb. Physiol. 54:103-200. http://dx.doi.org/10.1016 /S0065-2911(08)00002-7.
    • (2009) Adv. Microb. Physiol. , vol.54 , pp. 103-200
    • Frigaard, N.-U.1    Dahl, C.2
  • 3
    • 33747879596 scopus 로고    scopus 로고
    • Family I. Chromatiaceae Bavendamm 1924, 125AL emend. Imhoff 1984b, 339
    • Brenner DJ, Krieg NR, Staley JT, Garrity GM (ed), Springer, New York, NY
    • AL emend. Imhoff 1984b, 339, p 3-40. In Brenner DJ, Krieg NR, Staley JT, Garrity GM (ed), Bergey's manual of systematic bacteriology, vol 2. Springer, New York, NY.
    • (2005) Bergey's manual of systematic bacteriology , vol.2 , pp. 3-40
    • Imhoff, J.F.1
  • 4
    • 0029097501 scopus 로고
    • Development of a genetic system for a purple sulfur bacterium: conjugative plasmid transfer in Chromatium vinosum
    • Pattaragulwanit K, Dahl C. 1995. Development of a genetic system for a purple sulfur bacterium: conjugative plasmid transfer in Chromatium vinosum. Arch. Microbiol. 164:217-222. http://dx.doi.org/10.1007/BF02529974.
    • (1995) Arch. Microbiol. , vol.164 , pp. 217-222
    • Pattaragulwanit, K.1    Dahl, C.2
  • 5
    • 0030459663 scopus 로고    scopus 로고
    • Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum
    • Dahl C. 1996. Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum. Microbiology 142:3363-3372. http://dx.doi.org/10.1099/13500872-142 -12-3363.
    • (1996) Microbiology , vol.142 , pp. 3363-3372
    • Dahl, C.1
  • 8
    • 77957049802 scopus 로고    scopus 로고
    • DsrJ, an essential part of the DsrMKJOP complex in the purple sulfur bacterium Allochromatium vinosum, is an unusual triheme cytochrome c
    • Grein F, Venceslau SS, Schneider L, Hildebrandt P, Todorovic S, Pereira IAC, Dahl C. 2010. DsrJ, an essential part of the DsrMKJOP complex in the purple sulfur bacterium Allochromatium vinosum, is an unusual triheme cytochrome c. Biochemistry 49:8290-8299. http://dx .doi.org/10.1021/bi1007673.
    • (2010) Biochemistry , vol.49 , pp. 8290-8299
    • Grein, F.1    Venceslau, S.S.2    Schneider, L.3    Hildebrandt, P.4    Todorovic, S.5    Pereira, I.A.C.6    Dahl, C.7
  • 9
    • 33749989029 scopus 로고    scopus 로고
    • Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum
    • Hensen D, Sperling D, Trüper HG, Brune DC, Dahl C. 2006. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol. Microbiol. 62:794-810. http://dx.doi.org/10.1111/j.1365 -2958.2006.05408.x.
    • (2006) Mol. Microbiol. , vol.62 , pp. 794-810
    • Hensen, D.1    Sperling, D.2    Trüper, H.G.3    Brune, D.C.4    Dahl, C.5
  • 10
    • 0031864741 scopus 로고    scopus 로고
    • Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum
    • Reinartz M, Tschäpe J, Brüser T, Trüper HG, Dahl C. 1998. Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum. Arch. Microbiol. 170:59-68. http://dx.doi.org/10.1007/s002030050615.
    • (1998) Arch. Microbiol. , vol.170 , pp. 59-68
    • Reinartz, M.1    Tschäpe, J.2    Brüser, T.3    Trüper, H.G.4    Dahl, C.5
  • 11
    • 80052907486 scopus 로고    scopus 로고
    • Mechanisms and evolution of oxidative sulfur metabolism in green sulfur bacteria
    • Gregersen LH, Bryant DA, Frigaard N-U. 2011. Mechanisms and evolution of oxidative sulfur metabolism in green sulfur bacteria. Front. Microbiol. 2:116. http://dx.doi.org/10.3389/fmicb.2011.00116.
    • (2011) Front. Microbiol. , vol.2 , pp. 116
    • Gregersen, L.H.1    Bryant, D.A.2    Frigaard, N.-U.3
  • 12
    • 64049103790 scopus 로고    scopus 로고
    • Interaction between Sox proteins of two physiologically distinct bacteria and a new protein involved in thiosulfate oxidation
    • Welte C, Hafner S, Krätzer C, Quentmeier AT, Friedrich CG, Dahl C. 2009. Interaction between Sox proteins of two physiologically distinct bacteria and a new protein involved in thiosulfate oxidation. FEBS Lett. 583:1281-1286. http://dx.doi.org/10.1016/j.febslet.2009.03.020.
    • (2009) FEBS Lett. , vol.583 , pp. 1281-1286
    • Welte, C.1    Hafner, S.2    Krätzer, C.3    Quentmeier, A.T.4    Friedrich, C.G.5    Dahl, C.6
  • 13
    • 84883278259 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the purple sulfur bacterium Allochromatium vinosum DSM 180T during growth on different reduced sulfur compounds
    • Weissgerber T, Dobler N, Polen T, Latus J, Stockdreher Y, Dahl C. 2013. Genome-wide transcriptional profiling of the purple sulfur bacterium Allochromatium vinosum DSM 180T during growth on different reduced sulfur compounds. J. Bacteriol. 195:4231-4245. http://dx.doi.org /10.1128/JB.00154-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 4231-4245
    • Weissgerber, T.1    Dobler, N.2    Polen, T.3    Latus, J.4    Stockdreher, Y.5    Dahl, C.6
  • 14
    • 0029022442 scopus 로고
    • Isolation and characterization of sulfur globule proteins from Chromatium vinosum and Thiocapsa roseopersicina
    • Brune DC. 1995. Isolation and characterization of sulfur globule proteins from Chromatium vinosum and Thiocapsa roseopersicina. Arch. Microbiol. 163:391-399. http://dx.doi.org/10.1007/BF00272127.
    • (1995) Arch. Microbiol. , vol.163 , pp. 391-399
    • Brune, D.C.1
  • 15
    • 0031946732 scopus 로고    scopus 로고
    • Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum
    • Pattaragulwanit K, Brune DC, Trüper HG, Dahl C. 1998. Molecular genetic evidence for extracytoplasmic localization of sulfur globules in Chromatium vinosum. Arch. Microbiol. 169:434-444. http://dx.doi.org /10.1007/s002030050594.
    • (1998) Arch. Microbiol. , vol.169 , pp. 434-444
    • Pattaragulwanit, K.1    Brune, D.C.2    Trüper, H.G.3    Dahl, C.4
  • 16
    • 5444276327 scopus 로고    scopus 로고
    • The role of the sulfur globule proteins of Allochromatium vinosum: mutagenesis of the sulfur globule protein genes and expression studies by real-time RT PCR
    • Prange A, Engelhardt H, Trüper HG, Dahl C. 2004. The role of the sulfur globule proteins of Allochromatium vinosum: mutagenesis of the sulfur globule protein genes and expression studies by real-time RT PCR. Arch. Microbiol. 182:165-174. http://dx.doi.org/10.1007/s00203-004-0683-3.
    • (2004) Arch. Microbiol. , vol.182 , pp. 165-174
    • Prange, A.1    Engelhardt, H.2    Trüper, H.G.3    Dahl, C.4
  • 17
    • 0031855745 scopus 로고    scopus 로고
    • Sirohaem-sulfite reductase and other proteins encoded in the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
    • Pott AS, Dahl C. 1998. Sirohaem-sulfite reductase and other proteins encoded in the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. Microbiology 144:1881-1894. http://dx.doi .org/10.1099/00221287-144-7-1881.
    • (1998) Microbiology , vol.144 , pp. 1881-1894
    • Pott, A.S.1    Dahl, C.2
  • 18
    • 14544272337 scopus 로고    scopus 로고
    • Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum
    • Dahl C, Engels S, Pott-Sperling AS, Schulte A, Sander J, Lübbe Y, Deuster O, Brune DC. 2005. Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum. J. Bacteriol. 187:1392-1404. http://dx.doi.org/10.1128/JB.187.4.1392-1404.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 1392-1404
    • Dahl, C.1    Engels, S.2    Pott-Sperling, A.S.3    Schulte, A.4    Sander, J.5    Lübbe, Y.6    Deuster, O.7    Brune, D.C.8
  • 19
    • 84864008329 scopus 로고    scopus 로고
    • Cytoplasmic sulfurtransferases in the purple sulfur bacterium Allochromatium vinosum: evidence for sulfur transfer from DsrEFH to DsrC
    • Stockdreher Y, Venceslau SS, Josten M, Sahl HG, Pereira IAC, Dahl C. 2012. Cytoplasmic sulfurtransferases in the purple sulfur bacterium Allochromatium vinosum: evidence for sulfur transfer from DsrEFH to DsrC. PLoS One 7:e40785. http://dx.doi.org/10.1371/journal.pone.0040785.
    • (2012) PLoS One , vol.7
    • Stockdreher, Y.1    Venceslau, S.S.2    Josten, M.3    Sahl, H.G.4    Pereira, I.A.C.5    Dahl, C.6
  • 20
    • 50149094697 scopus 로고    scopus 로고
    • Allochromatium vinosum DsrC: solution-state NMR structure, redox properties and interaction with DsrEFH, a protein essential for purple sulfur bacterial sulfur oxidation
    • Cort JR, Selan UM, Schulte A, Grimm F, Kennedy MA, Dahl C. 2008. Allochromatium vinosum DsrC: solution-state NMR structure, redox properties and interaction with DsrEFH, a protein essential for purple sulfur bacterial sulfur oxidation. J. Mol. Biol. 382:692-707. http://dx.doi .org/10.1016/j.jmb.2008.07.022.
    • (2008) J. Mol. Biol. , vol.382 , pp. 692-707
    • Cort, J.R.1    Selan, U.M.2    Schulte, A.3    Grimm, F.4    Kennedy, M.A.5    Dahl, C.6
  • 21
    • 57749097713 scopus 로고    scopus 로고
    • The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration
    • Oliveira TF, Vonrhein C, Matia PM, Venceslau SS, Pereira IAC, Archer M. 2008. The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration. J. Biol. Chem. 283:34141-34149. http://dx.doi.org /10.1074/jbc.M805643200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34141-34149
    • Oliveira, T.F.1    Vonrhein, C.2    Matia, P.M.3    Venceslau, S.S.4    Pereira, I.A.C.5    Archer, M.6
  • 22
    • 84888858723 scopus 로고    scopus 로고
    • Sulfite oxidation in the purple sulfur bacterium Allochromatium vinosum: identification of SoeABC as a major player and relevance of SoxYZ in the process
    • Dahl C, Franz B, Hensen D, Kesselheim A, Zigann R. 2013. Sulfite oxidation in the purple sulfur bacterium Allochromatium vinosum: identification of SoeABC as a major player and relevance of SoxYZ in the process. Microbiology 159:2626-2638. http://dx.doi.org/10.1099/mic.0 .071019-0.
    • (2013) Microbiology , vol.159 , pp. 2626-2638
    • Dahl, C.1    Franz, B.2    Hensen, D.3    Kesselheim, A.4    Zigann, R.5
  • 23
    • 0035731062 scopus 로고    scopus 로고
    • In vivo role of APS reductase in the purple sulfur bacterium Allochromatium vinosum
    • Sanchez O, Ferrera I, Dahl C, Mas J. 2001. In vivo role of APS reductase in the purple sulfur bacterium Allochromatium vinosum. Arch. Microbiol. 176:301-305. http://dx.doi.org/10.1007/s002030100327.
    • (2001) Arch. Microbiol. , vol.176 , pp. 301-305
    • Sanchez, O.1    Ferrera, I.2    Dahl, C.3    Mas, J.4
  • 24
    • 65549156552 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes)
    • Jendrossek D. 2009. Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes). J. Bacteriol. 191:3195-3202. http://dx .doi.org/10.1128/JB.01723-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 3195-3202
    • Jendrossek, D.1
  • 25
    • 0016720598 scopus 로고
    • Characterization of Rhodopseudomonas capsulata
    • Weaver PF, Wall JD, Gest H. 1975. Characterization of Rhodopseudomonas capsulata. Arch. Microbiol. 105:207-216. http://dx.doi.org/10 .1007/BF00447139.
    • (1975) Arch. Microbiol. , vol.105 , pp. 207-216
    • Weaver, P.F.1    Wall, J.D.2    Gest, H.3
  • 26
    • 34247196725 scopus 로고    scopus 로고
    • Utilization of solid "elemental" sulfur by the phototrophic purple sulfur bacterium Allochromatium vinosum: a sulfur K-edge XANES spectroscopy study
    • Franz B, Lichtenberg H, Hormes J, Modrow H, Dahl C, Prange A. 2007. Utilization of solid "elemental" sulfur by the phototrophic purple sulfur bacterium Allochromatium vinosum: a sulfur K-edge XANES spectroscopy study. Microbiology 153:1268-1274. http://dx.doi.org/10.1099/mic.0 .2006/003954-0.
    • (2007) Microbiology , vol.153 , pp. 1268-1274
    • Franz, B.1    Lichtenberg, H.2    Hormes, J.3    Modrow, H.4    Dahl, C.5    Prange, A.6
  • 28
    • 0029285787 scopus 로고
    • PCR mediated recombination and mutagenesis: SOEing together tailor-made genes
    • Horton RM. 1995. PCR mediated recombination and mutagenesis: SOEing together tailor-made genes. Mol. Biotechnol. 3:93-99. http://dx.doi .org/10.1007/BF02789105.
    • (1995) Mol. Biotechnol. , vol.3 , pp. 93-99
    • Horton, R.M.1
  • 29
    • 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. Nat. Biotechnol. 1:784-791. http://dx.doi.org/10.1038 /nbt1183-784.
    • (1983) Nat. Biotechnol. , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. http://dx.doi.org/10 .1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 84885106989 scopus 로고    scopus 로고
    • Quantitative assessment of in-solution digestion efficiency identifies optimal protocols for unbiased protein analysis
    • León IR, Schwämmle V, Jensen NO, Sprenger RR. 2013. Quantitative assessment of in-solution digestion efficiency identifies optimal protocols for unbiased protein analysis. Mol. Cell. Proteomics 12:2992-3005. http: //dx.doi.org/10.1074/mcp.M112.025585.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2992-3005
    • León, I.R.1    Schwämmle, V.2    Jensen, N.O.3    Sprenger, R.R.4
  • 32
    • 18844460394 scopus 로고    scopus 로고
    • Sample preparation and digestion for proteomic analyses using spin filters
    • Manza LL, Stamer SL, Ham AJL, Codreanu SG, Liebler DC. 2005. Sample preparation and digestion for proteomic analyses using spin filters. Proteomics 5:1742-1745. http://dx.doi.org/10.1002/pmic.200401063.
    • (2005) Proteomics , vol.5 , pp. 1742-1745
    • Manza, L.L.1    Stamer, S.L.2    Ham, A.J.L.3    Codreanu, S.G.4    Liebler, D.C.5
  • 33
    • 39749125069 scopus 로고    scopus 로고
    • Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis
    • Masuda T, Tomita M, Ishihama Y. 2008. Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis. J. Proteome Res. 7:731-740. http://dx.doi.org/10.1021/pr700658q.
    • (2008) J. Proteome Res. , vol.7 , pp. 731-740
    • Masuda, T.1    Tomita, M.2    Ishihama, Y.3
  • 34
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski JR, Zougman A, Nagaraj N, Mann M. 2009. Universal sample preparation method for proteome analysis. Nat. Methods 6:359-362. http://dx.doi.org/10.1038/nmeth.1322.
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 35
    • 33750685330 scopus 로고    scopus 로고
    • Importance of the DsrMKJOP complex for sulfur oxidation in Allochromatium vinosum and phylogenetic analysis of related complexes in other prokaryotes
    • Sander J, Engels-Schwarzlose S, Dahl C. 2006. Importance of the DsrMKJOP complex for sulfur oxidation in Allochromatium vinosum and phylogenetic analysis of related complexes in other prokaryotes. Arch. Microbiol. 186:357-366. http://dx.doi.org/10.1007/s00203-006-0156-y.
    • (2006) Arch. Microbiol. , vol.186 , pp. 357-366
    • Sander, J.1    Engels-Schwarzlose, S.2    Dahl, C.3
  • 36
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M. 2006. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1:2856-2860. http://dx.doi.org/10.1038/nprot.2006 .468.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 37
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after 1-dimensional or 2-dimensional gel electrophoresis
    • Rosenfeld J, Capdevielle J, Guillemot JC, Ferrara P. 1992. In-gel digestion of proteins for internal sequence analysis after 1-dimensional or 2-dimensional gel electrophoresis. Anal. Biochem. 203:173-179. http://dx.doi .org/10.1016/0003-2697(92)90061-B.
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 38
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu P, Vogel C, Wang R, Yao X, Marcotte EM. 2007. Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat. Biotechnol. 25:117-124. http://dx.doi .org/10.1038/nbt1270.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 39
    • 0017861127 scopus 로고
    • Patterns of protein synthesis in Escherichia coli: a catalog of amount of 140 individual proteins at different growth rates
    • Pedersen S, Bloch PL, Reeh S, Neidhardt FC. 1978. Patterns of protein synthesis in Escherichia coli: a catalog of amount of 140 individual proteins at different growth rates. Cell 14:179-190. http://dx.doi.org/10.1016/0092 -8674(78)90312-4.
    • (1978) Cell , vol.14 , pp. 179-190
    • Pedersen, S.1    Bloch, P.L.2    Reeh, S.3    Neidhardt, F.C.4
  • 40
    • 0037118719 scopus 로고    scopus 로고
    • The role of high-potential iron protein and cytochrome c8 as alternative electron donors to the reaction center of Chromatium vinosum
    • Verméglio A, Li J, Schoepp-Cothenet B, Pratt N, Knaff DB. 2002. The role of high-potential iron protein and cytochrome c8 as alternative electron donors to the reaction center of Chromatium vinosum. Biochemistry 41:8868-8875. http://dx.doi.org/10.1021/bi012037h.
    • (2002) Biochemistry , vol.41 , pp. 8868-8875
    • Verméglio, A.1    Li, J.2    Schoepp-Cothenet, B.3    Pratt, N.4    Knaff, D.B.5
  • 41
    • 0018966715 scopus 로고
    • Malic enzyme of Chromatium vinosum
    • Sahl HG, Trüper HG. 1980. Malic enzyme of Chromatium vinosum. Arch. Microbiol. 127:17-24. http://dx.doi.org/10.1007/BF00414350.
    • (1980) Arch. Microbiol. , vol.127 , pp. 17-24
    • Sahl, H.G.1    Trüper, H.G.2
  • 42
    • 56949086026 scopus 로고    scopus 로고
    • Structural and molecular genetic insight into a wide-spread bacterial sulfur oxidation pathway
    • Dahl C, Schulte A, Stockdreher Y, Hong C, Grimm F, Sander J, Kim R, Kim S-H, Shin DH. 2008. Structural and molecular genetic insight into a wide-spread bacterial sulfur oxidation pathway. J. Mol. Biol. 384:1287-1300. http://dx.doi.org/10.1016/j.jmb.2008.10.016.
    • (2008) J. Mol. Biol. , vol.384 , pp. 1287-1300
    • Dahl, C.1    Schulte, A.2    Stockdreher, Y.3    Hong, C.4    Grimm, F.5    Sander, J.6    Kim, R.7    Kim, S.-H.8    Shin, D.H.9
  • 43
    • 0034156863 scopus 로고    scopus 로고
    • Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway
    • Neumann S, Wynen A, Trüper HG, Dahl C. 2000. Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway. Mol. Biol. Rep. 27:27-33. http://dx.doi.org /10.1023/A:1007058421714.
    • (2000) Mol. Biol. Rep. , vol.27 , pp. 27-33
    • Neumann, S.1    Wynen, A.2    Trüper, H.G.3    Dahl, C.4
  • 44
    • 0022114244 scopus 로고
    • A survey of buoyant density of microorganisms in pure cultures and natural samples
    • Guerrero R, Pedros-Alio C, Schmidt TM, Mas J. 1985. A survey of buoyant density of microorganisms in pure cultures and natural samples. Microbiologia 1:53-65.
    • (1985) Microbiologia , vol.1 , pp. 53-65
    • Guerrero, R.1    Pedros-Alio, C.2    Schmidt, T.M.3    Mas, J.4
  • 45
    • 0025052297 scopus 로고
    • Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/ oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum
    • Viale AM, Kobayashi H, Akazawa T. 1990. Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/ oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum. J. Biol. Chem. 265:18386-18392.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18386-18392
    • Viale, A.M.1    Kobayashi, H.2    Akazawa, T.3
  • 46
    • 0024672740 scopus 로고
    • Expressed genes for planttype ribulose 1,5-bisphosphate carboxylase/oxygenase in the photosynthetic bacterium Chromatium vinosum, which possesses two complete sets of genes
    • Viale AM, Kobayashi H, Akazawa T. 1989. Expressed genes for planttype ribulose 1,5-bisphosphate carboxylase/oxygenase in the photosynthetic bacterium Chromatium vinosum, which possesses two complete sets of genes. J. Bacteriol. 171:2391-2400.
    • (1989) J. Bacteriol. , vol.171 , pp. 2391-2400
    • Viale, A.M.1    Kobayashi, H.2    Akazawa, T.3
  • 47
    • 70349661794 scopus 로고    scopus 로고
    • Carbohydrate metabolism and carbon fixation in Roseobacter denitrificans OCh114
    • Tang KH, Feng XY, Tang YJJ, Blankenship RE. 2009. Carbohydrate metabolism and carbon fixation in Roseobacter denitrificans OCh114. PLoS One 4:e7233. http://dx.doi.org/10.1371/journal.pone.0007233.
    • (2009) PLoS One , vol.4
    • Tang, K.H.1    Feng, X.Y.2    Tang, Y.J.J.3    Blankenship, R.E.4
  • 49
    • 0141479523 scopus 로고
    • Aspects of terminal respiration in microorganisms
    • Kornberg HL. 1959. Aspects of terminal respiration in microorganisms. Annu. Rev. Microbiol. 13:49-78. http://dx.doi.org/10.1146/annurev.mi .13.100159.000405.
    • (1959) Annu. Rev. Microbiol. , vol.13 , pp. 49-78
    • Kornberg, H.L.1
  • 50
    • 84879262130 scopus 로고    scopus 로고
    • The carbon storage regulator (Csr) system exerts a nutrient-specific control over central metabolism in Escherichia coli strain Nissle 1917
    • Revelles O, Millard P, Nougayrede JP, Dobrindt U, Oswald E, Letisse F, Portais JC. 2013. The carbon storage regulator (Csr) system exerts a nutrient-specific control over central metabolism in Escherichia coli strain Nissle 1917. PLoS One 8:e66386. http://dx.doi.org/10.1371/journal.pone .0066386.
    • (2013) PLoS One , vol.8
    • Revelles, O.1    Millard, P.2    Nougayrede, J.P.3    Dobrindt, U.4    Oswald, E.5    Letisse, F.6    Portais, J.C.7
  • 51
    • 84873165273 scopus 로고    scopus 로고
    • Post-transcriptional regulation on a global scale: form and function of Csr/Rsm systems
    • Romeo T, Vakulskas CA, Babitzke P. 2013. Post-transcriptional regulation on a global scale: form and function of Csr/Rsm systems. Environ. Microbiol. 15:313-324. http://dx.doi.org/10.1111/j.1462-2920.2012.02794.x.
    • (2013) Environ. Microbiol. , vol.15 , pp. 313-324
    • Romeo, T.1    Vakulskas, C.A.2    Babitzke, P.3
  • 52
    • 62649103362 scopus 로고    scopus 로고
    • Conditional essentiality of the csrA gene in Escherichia coli
    • Timmermans J, Van Melderen L. 2009. Conditional essentiality of the csrA gene in Escherichia coli. J. Bacteriol. 191:1722-1724. http://dx.doi.org /10.1128/JB.01573-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 1722-1724
    • Timmermans, J.1    Van Melderen, L.2
  • 53
    • 84884484623 scopus 로고    scopus 로고
    • Structural, biochemical and genetic characterization of ATP sulfurylase from Allochromatium vinosum
    • Parey K, Demmer U, Warkentin E, Wynen A, Ermler U, Dahl C. 2013. Structural, biochemical and genetic characterization of ATP sulfurylase from Allochromatium vinosum. PLoS One 8:e74707. http://dx.doi.org/10 .1371/journal.pone.0074707.
    • (2013) PLoS One , vol.8
    • Parey, K.1    Demmer, U.2    Warkentin, E.3    Wynen, A.4    Ermler, U.5    Dahl, C.6
  • 54
    • 0030821694 scopus 로고    scopus 로고
    • Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes
    • Hipp WM, Pott AS, Thum-Schmitz N, Faath I, Dahl C, Trüper HG. 1997. Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes. Microbiology 143:2891-2902. http://dx.doi.org/10.1099/00221287-143-9-2891.
    • (1997) Microbiology , vol.143 , pp. 2891-2902
    • Hipp, W.M.1    Pott, A.S.2    Thum-Schmitz, N.3    Faath, I.4    Dahl, C.5    Trüper, H.G.6
  • 55
    • 0141814895 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens
    • Laska S, Lottspeich F, Kletzin A. 2003. Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens. Microbiology 149:2357-2371. http://dx.doi.org/10 .1099/mic.0.26455-0.
    • (2003) Microbiology , vol.149 , pp. 2357-2371
    • Laska, S.1    Lottspeich, F.2    Kletzin, A.3
  • 56
    • 84872165430 scopus 로고    scopus 로고
    • Chlorobaculum tepidum TLS displays a complex transcriptional response to sulfide addition
    • Eddie BJ, Hanson TE. 2013. Chlorobaculum tepidum TLS displays a complex transcriptional response to sulfide addition. J. Bacteriol. 195:399-408. http://dx.doi.org/10.1128/JB.01342-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 399-408
    • Eddie, B.J.1    Hanson, T.E.2
  • 57
    • 0035877729 scopus 로고    scopus 로고
    • Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling
    • Vergauwen B, Pauwels F, Jacquemotte F, Meyer TE, Cusanovich MA, Bartsch RG, van Beeumen JJ. 2001. Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling. J. Biol. Chem. 276:20890-20897. http://dx.doi.org/10.1074/jbc.M102026200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20890-20897
    • Vergauwen, B.1    Pauwels, F.2    Jacquemotte, F.3    Meyer, T.E.4    Cusanovich, M.A.5    Bartsch, R.G.6    van Beeumen, J.J.7
  • 58
    • 84866139470 scopus 로고    scopus 로고
    • Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU)
    • Kim JH, Tonelli M, Frederick RO, Chow DC, Markley JL. 2012. Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU). J. Biol. Chem. 287: 31406-31413. http://dx.doi.org/10.1074/jbc.M112.352617.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31406-31413
    • Kim, J.H.1    Tonelli, M.2    Frederick, R.O.3    Chow, D.C.4    Markley, J.L.5
  • 59
    • 33746488266 scopus 로고    scopus 로고
    • Siro(haem)amide in Allochromatium vinosum and relevance of DsrL and DsrN, a homolog of cobyrinic acid a,c diamide synthase for sulphur oxidation
    • Lübbe YJ, Youn H-S, Timkovich R, Dahl C. 2006. Siro(haem)amide in Allochromatium vinosum and relevance of DsrL and DsrN, a homolog of cobyrinic acid a,c diamide synthase for sulphur oxidation. FEMS Microbiol. Lett. 261:194-202. http://dx.doi.org/10.1111/j.1574 -6968.2006.00343.x.
    • (2006) FEMS Microbiol. Lett. , vol.261 , pp. 194-202
    • Lübbe, Y.J.1    Youn, H.-S.2    Timkovich, R.3    Dahl, C.4
  • 60
    • 77749243497 scopus 로고    scopus 로고
    • Regulation of dsr genes encoding proteins responsible for the oxidation of stored sulfur in Allochromatium vinosum
    • Grimm F, Dobler N, Dahl C. 2010. Regulation of dsr genes encoding proteins responsible for the oxidation of stored sulfur in Allochromatium vinosum. Microbiology 156:764-773. http://dx.doi.org/10.1099/mic.0 .034645-0.
    • (2010) Microbiology , vol.156 , pp. 764-773
    • Grimm, F.1    Dobler, N.2    Dahl, C.3
  • 63
    • 84862223771 scopus 로고    scopus 로고
    • Evolution and diversification of group 1 [NiFe] hydrogenases. Is there a phylogenetic marker for O2-tolerance?
    • Pandelia M-E, Lubitz W, Nitschke W. 2012. Evolution and diversification of group 1 [NiFe] hydrogenases. Is there a phylogenetic marker for O2-tolerance? Biochim. Biophys. Acta 1817:1565-1575. http://dx.doi.org /10.1016/j.bbabio.2012.04.012.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1565-1575
    • Pandelia, M.-E.1    Lubitz, W.2    Nitschke, W.3
  • 65
    • 0028946435 scopus 로고
    • Characterization of the locus encoding the [NiFe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases
    • Pedroni P, della Volpe A, Galli G, Mura GM, Pratesi C, Grandi G. 1995. Characterization of the locus encoding the [NiFe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases. Microbiology 141:449-458. http://dx.doi.org/10.1099 /13500872-141-2-449.
    • (1995) Microbiology , vol.141 , pp. 449-458
    • Pedroni, P.1    della Volpe, A.2    Galli, G.3    Mura, G.M.4    Pratesi, C.5    Grandi, G.6
  • 66
    • 0032779210 scopus 로고    scopus 로고
    • On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry
    • Silva PJ, de Castro B, Hagen WR. 1999. On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry. J. Biol. Inorg. Chem. 4:284-291. http://dx.doi.org/10.1007/s007750050314.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 284-291
    • Silva, P.J.1    de Castro, B.2    Hagen, W.R.3
  • 67
    • 34548687266 scopus 로고    scopus 로고
    • 2 evolution/consumption reactions, mediated by various hydrogenases, in the purple sulfur bacterium, Thiocapsa roseopersicina
    • 2 evolution/consumption reactions, mediated by various hydrogenases, in the purple sulfur bacterium, Thiocapsa roseopersicina. Arch. Microbiol. 188:403-410. http://dx.doi.org/10.1007 /s00203-007-0260-7.
    • (2007) Arch. Microbiol. , vol.188 , pp. 403-410
    • Laurinavichene, T.V.1    Rákhely, G.2    Kovács, K.L.3    Tsygankov, A.A.4
  • 68
    • 70350445731 scopus 로고    scopus 로고
    • Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans
    • Quatrini R, Appia-Ayme C, Denis Y, Jedlicki E, Holmes DS, Bonnefoy V. 2009. Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans. BMC Genomics 10:394. http://dx.doi.org/10.1186/1471-2164-10-394.
    • (2009) BMC Genomics , vol.10 , pp. 394
    • Quatrini, R.1    Appia-Ayme, C.2    Denis, Y.3    Jedlicki, E.4    Holmes, D.S.5    Bonnefoy, V.6
  • 69
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Vandyke M, Stock J. 1991. Predicting coiled coils from protein sequences. Science 252:1162-1164. http://dx.doi.org/10.1126/science.252 .5009.1162.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Vandyke, M.2    Stock, J.3
  • 70
    • 4344685822 scopus 로고    scopus 로고
    • Scaffolds, levers, rods and springs: diverse cellular functions of long coiled-coil proteins
    • Rose A, Meier I. 2004. Scaffolds, levers, rods and springs: diverse cellular functions of long coiled-coil proteins. Cell. Mol. Life Sci. 61:1996-2009. http://dx.doi.org/10.1007/s00018-004-4039-6.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1996-2009
    • Rose, A.1    Meier, I.2
  • 71
    • 84883195057 scopus 로고    scopus 로고
    • Nucleotide-independent cytoskeletal scaffolds in bacteria
    • Lin L, Thanbichler M. 2013. Nucleotide-independent cytoskeletal scaffolds in bacteria. Cytoskeleton 70:409-423. http://dx.doi.org/10.1002/cm .21126.
    • (2013) Cytoskeleton , vol.70 , pp. 409-423
    • Lin, L.1    Thanbichler, M.2

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