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Volumn 7, Issue 4, 2012, Pages

The ruegeria pomeroyi acui gene has a role in DMSP catabolism and resembles yhdH of E. coli and other bacteria in conferring resistance to acrylate

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLIC ACID; DIMETHYL SULFIDE; DIMETHYL SULFONE; ESCHERICHIA COLI YHDH POLYPEPTIDE; HYDRACRYLIC ACID; POLYPEPTIDE; UNCLASSIFIED DRUG; ACRYLIC ACID DERIVATIVE; ACRYLOYL COENZYME A REDUCTASE; ACRYLOYL-COA REDUCTASE; BACTERIAL PROTEIN; DIMETHYLPROPIOTHETIN; DIMETHYLSULFONIOPROPIONATE LYASE; ESCHERICHIA COLI PROTEIN; LYASE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SULFONIUM DERIVATIVE; YHDH PROTEIN, E COLI;

EID: 84860379615     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035947     Document Type: Article
Times cited : (45)

References (59)
  • 1
    • 0033828996 scopus 로고    scopus 로고
    • Physiological aspects of the production and conversion of DMSP in marine algae and higher plants
    • Stefels J, (2000) Physiological aspects of the production and conversion of DMSP in marine algae and higher plants. J Sea Res 43: 183-197.
    • (2000) J Sea Res , vol.43 , pp. 183-197
    • Stefels, J.1
  • 2
    • 4344715431 scopus 로고    scopus 로고
    • Dimethylsulphoniopropionate (DMSP) and related compounds in higher plants
    • Otte ML, Wilson G, Morris JT, Moran BM, (2004) Dimethylsulphoniopropionate (DMSP) and related compounds in higher plants. J Exp Bot 55: 1919-1925.
    • (2004) J Exp Bot , vol.55 , pp. 1919-1925
    • Otte, M.L.1    Wilson, G.2    Morris, J.T.3    Moran, B.M.4
  • 3
    • 0033832734 scopus 로고    scopus 로고
    • New and important roles for DMSP in marine microbial communities
    • Kiene RP, Linn LJ, Bruton JA, (2000) New and important roles for DMSP in marine microbial communities. Journal of Sea Research 43: 209-224.
    • (2000) Journal of Sea Research , vol.43 , pp. 209-224
    • Kiene, R.P.1    Linn, L.J.2    Bruton, J.A.3
  • 4
  • 5
    • 0036952070 scopus 로고    scopus 로고
    • Dimethylsulfoniopropionate: Its sources, role in the marine food web, and biological degradation to dimethyl sulfide
    • Yoch DC, (2002) Dimethylsulfoniopropionate: Its sources, role in the marine food web, and biological degradation to dimethyl sulfide. Appl Env Microbiol 68: 5804-5815.
    • (2002) Appl Env Microbiol , vol.68 , pp. 5804-5815
    • Yoch, D.C.1
  • 6
    • 81255171219 scopus 로고    scopus 로고
    • Catabolism of dimethylsulphoniopropionate: microorganisms, enzymes and genes
    • Curson AR, Todd JD, Sullivan MJ, Johnston AW, (2011) Catabolism of dimethylsulphoniopropionate: microorganisms, enzymes and genes. Nat Rev Microbiol 9: 849-859.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 849-859
    • Curson, A.R.1    Todd, J.D.2    Sullivan, M.J.3    Johnston, A.W.4
  • 7
    • 81255193677 scopus 로고    scopus 로고
    • Bacterial Catabolism of Dimethylsulfoniopropionate (DMSP)
    • Reisch CR, Moran MA, Whitman WB, (2011) Bacterial Catabolism of Dimethylsulfoniopropionate (DMSP). Front Microbiol 2: 172.
    • (2011) Front Microbiol , vol.2 , pp. 172
    • Reisch, C.R.1    Moran, M.A.2    Whitman, W.B.3
  • 8
    • 77649108665 scopus 로고    scopus 로고
    • Molecular dissection of bacterial acrylate catabolism-unexpected links with dimethylsulfoniopropionate catabolism and dimethyl sulfide production
    • Todd JD, Curson AR, Nikolaidou-Katsaraidou N, Brearley CA, Watmough NJ, et al. (2010) Molecular dissection of bacterial acrylate catabolism-unexpected links with dimethylsulfoniopropionate catabolism and dimethyl sulfide production. Environ Microbiol 12: 327-343.
    • (2010) Environ Microbiol , vol.12 , pp. 327-343
    • Todd, J.D.1    Curson, A.R.2    Nikolaidou-Katsaraidou, N.3    Brearley, C.A.4    Watmough, N.J.5
  • 10
    • 79955894948 scopus 로고    scopus 로고
    • Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria
    • Reisch CR, Stoudemayer MJ, Varaljay VA, Amster IJ, Moran MA, et al. (2011) Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria. Nature 473: 208-211.
    • (2011) Nature , vol.473 , pp. 208-211
    • Reisch, C.R.1    Stoudemayer, M.J.2    Varaljay, V.A.3    Amster, I.J.4    Moran, M.A.5
  • 11
    • 79251577109 scopus 로고    scopus 로고
    • Unusual regulation of a leaderless operon involved in the catabolism of dimethylsulfoniopropionate in Rhodobacter sphaeroides
    • Sullivan MJ, Curson AR, Shearer N, Todd JD, Green RT, et al. (2011) Unusual regulation of a leaderless operon involved in the catabolism of dimethylsulfoniopropionate in Rhodobacter sphaeroides. PLoS One 6: e15972.
    • (2011) PLoS One , vol.6
    • Sullivan, M.J.1    Curson, A.R.2    Shearer, N.3    Todd, J.D.4    Green, R.T.5
  • 12
    • 38549098458 scopus 로고    scopus 로고
    • Molecular genetic analysis of a dimethylsulfoniopropionate lyase that liberates the climate-changing gas dimethylsulfide in several marine alpha-proteobacteria and Rhodobacter sphaeroides
    • Curson AR, Rogers R, Todd JD, Brearley CA, Johnston AW, (2008) Molecular genetic analysis of a dimethylsulfoniopropionate lyase that liberates the climate-changing gas dimethylsulfide in several marine alpha-proteobacteria and Rhodobacter sphaeroides. Environ Microbiol 10: 757-767.
    • (2008) Environ Microbiol , vol.10 , pp. 757-767
    • Curson, A.R.1    Rogers, R.2    Todd, J.D.3    Brearley, C.A.4    Johnston, A.W.5
  • 13
    • 84855872335 scopus 로고    scopus 로고
    • Rhodobacter sphaeroides uses a reductive route via propionyl-CoA to assimilate 3-hydroxypropionate
    • Schneider K, Asao M, Carter MS, Alber BE, (2012) Rhodobacter sphaeroides uses a reductive route via propionyl-CoA to assimilate 3-hydroxypropionate. J Bact 194: 225-232.
    • (2012) J Bact , vol.194 , pp. 225-232
    • Schneider, K.1    Asao, M.2    Carter, M.S.3    Alber, B.E.4
  • 14
    • 77958463670 scopus 로고    scopus 로고
    • Subdivision of the MDR superfamily of medium-chain dehydrogenases/reductases through iterative hidden Markov model refinement
    • Hedlund J, Jornvall H, Persson B, (2010) Subdivision of the MDR superfamily of medium-chain dehydrogenases/reductases through iterative hidden Markov model refinement. BMC Bioinformatics 11: 534.
    • (2010) BMC Bioinformatics , vol.11 , pp. 534
    • Hedlund, J.1    Jornvall, H.2    Persson, B.3
  • 16
    • 77952309568 scopus 로고    scopus 로고
    • Superfamilies SDR and MDR: from early ancestry to present forms. Emergence of three lines, a Zn-metalloenzyme, and distinct variabilities
    • Jornvall H, Hedlund J, Bergman T, Oppermann U, Persson B, (2010) Superfamilies SDR and MDR: from early ancestry to present forms. Emergence of three lines, a Zn-metalloenzyme, and distinct variabilities. Biochem Biophys Res Commun 396: 125-130.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 125-130
    • Jornvall, H.1    Hedlund, J.2    Bergman, T.3    Oppermann, U.4    Persson, B.5
  • 17
    • 0041029935 scopus 로고    scopus 로고
    • Transformation of sulfur compounds by an abundant lineage of marine bacteria in the alpha-subclass of the class Proteobacteria
    • Gonzalez JM, Kiene RP, Moran MA, (1999) Transformation of sulfur compounds by an abundant lineage of marine bacteria in the alpha-subclass of the class Proteobacteria. Appl Environ Microbiol 65: 3810-3819.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3810-3819
    • Gonzalez, J.M.1    Kiene, R.P.2    Moran, M.A.3
  • 18
    • 77952674525 scopus 로고    scopus 로고
    • Genome characteristics of a generalist marine bacterial lineage
    • Newton RJ, Griffin LE, Bowles KM, Meile C, Gifford S, et al. (2010) Genome characteristics of a generalist marine bacterial lineage. ISME J 4: 784-798.
    • (2010) ISME J , vol.4 , pp. 784-798
    • Newton, R.J.1    Griffin, L.E.2    Bowles, K.M.3    Meile, C.4    Gifford, S.5
  • 19
    • 33846820411 scopus 로고    scopus 로고
    • Structural and regulatory genes required to make the gas dimethyl sulfide in bacteria
    • Todd JD, Rogers R, Li YG, Wexler M, Bond PL, et al. (2007) Structural and regulatory genes required to make the gas dimethyl sulfide in bacteria. Science 315: 666-669.
    • (2007) Science , vol.315 , pp. 666-669
    • Todd, J.D.1    Rogers, R.2    Li, Y.G.3    Wexler, M.4    Bond, P.L.5
  • 20
    • 79959622728 scopus 로고    scopus 로고
    • DddY, a periplasmic dimethylsulfoniopropionate lyase found in taxonomically diverse species of Proteobacteria
    • Curson AR, Sullivan MJ, Todd JD, Johnston AW, (2011) DddY, a periplasmic dimethylsulfoniopropionate lyase found in taxonomically diverse species of Proteobacteria. ISME J 5: 1191-1200.
    • (2011) ISME J , vol.5 , pp. 1191-1200
    • Curson, A.R.1    Sullivan, M.J.2    Todd, J.D.3    Johnston, A.W.4
  • 21
    • 0028878784 scopus 로고
    • Purification and characterization of dimethylsulfoniopropionate lyase from an alcaligenes-like dimethyl sulfide-producing marine isolate
    • de Souza MP, Yoch DC, (1995) Purification and characterization of dimethylsulfoniopropionate lyase from an alcaligenes-like dimethyl sulfide-producing marine isolate. Appl Environ Microbiol 61: 21-26.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 21-26
    • de Souza, M.P.1    Yoch, D.C.2
  • 22
    • 66649103701 scopus 로고    scopus 로고
    • The dddP gene, encoding a novel enzyme that converts dimethylsulfoniopropionate into dimethyl sulfide, is widespread in ocean metagenomes and marine bacteria and also occurs in some Ascomycete fungi
    • Todd JD, Curson AR, Dupont CL, Nicholson P, Johnston AW, (2009) The dddP gene, encoding a novel enzyme that converts dimethylsulfoniopropionate into dimethyl sulfide, is widespread in ocean metagenomes and marine bacteria and also occurs in some Ascomycete fungi. Environ Microbiol 11: 1376-1385.
    • (2009) Environ Microbiol , vol.11 , pp. 1376-1385
    • Todd, J.D.1    Curson, A.R.2    Dupont, C.L.3    Nicholson, P.4    Johnston, A.W.5
  • 24
    • 79551501392 scopus 로고    scopus 로고
    • DddQ, a novel, cupin-containing, dimethylsulfoniopropionate lyase in marine roseobacters and in uncultured marine bacteria
    • Todd JD, Curson AR, Kirkwood M, Sullivan MJ, Green RT, et al. (2011) DddQ, a novel, cupin-containing, dimethylsulfoniopropionate lyase in marine roseobacters and in uncultured marine bacteria. Environ Microbiol 13: 427-438.
    • (2011) Environ Microbiol , vol.13 , pp. 427-438
    • Todd, J.D.1    Curson, A.R.2    Kirkwood, M.3    Sullivan, M.J.4    Green, R.T.5
  • 25
    • 84355161790 scopus 로고    scopus 로고
    • DddW, a third DMSP lyase in a model Roseobacter marine bacterium, Ruegeria pomeroyi DSS-3
    • Todd JD, Kirkwood M, Newton-Payne S, Johnston AW, (2012) DddW, a third DMSP lyase in a model Roseobacter marine bacterium, Ruegeria pomeroyi DSS-3. ISME J 6: 223-226.
    • (2012) ISME J , vol.6 , pp. 223-226
    • Todd, J.D.1    Kirkwood, M.2    Newton-Payne, S.3    Johnston, A.W.4
  • 26
    • 78751503218 scopus 로고    scopus 로고
    • Complete genome sequence of Arcobacter nitrofigilis type strain (CI)
    • Pati A, Gronow S, Lapidus A, Copeland A, Glavina Del Rio T, et al. (2010) Complete genome sequence of Arcobacter nitrofigilis type strain (CI). Stand Genomic Sci 2: 300-308.
    • (2010) Stand Genomic Sci , vol.2 , pp. 300-308
    • Pati, A.1    Gronow, S.2    Lapidus, A.3    Copeland, A.4    Del Rio, T.G.5
  • 27
    • 0035930701 scopus 로고    scopus 로고
    • Miniature genome in the marine chordate Oikopleura dioica
    • Seo HC, Kube M, Edvardsen RB, Jensen MF, Beck A, et al. (2001) Miniature genome in the marine chordate Oikopleura dioica. Science 294: 2506.
    • (2001) Science , vol.294 , pp. 2506
    • Seo, H.C.1    Kube, M.2    Edvardsen, R.B.3    Jensen, M.F.4    Beck, A.5
  • 28
    • 19944408938 scopus 로고    scopus 로고
    • Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment
    • Moran MA, Buchan A, Gonzalez JM, Heidelberg JF, Whitman WB, et al. (2004) Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment. Nature 432: 910-913.
    • (2004) Nature , vol.432 , pp. 910-913
    • Moran, M.A.1    Buchan, A.2    Gonzalez, J.M.3    Heidelberg, J.F.4    Whitman, W.B.5
  • 29
    • 33748675283 scopus 로고
    • Atmospheric dimethyl sulphide and the natural sulphur cycle
    • Lovelock JE, Maggs RJ, Rasmussen RA, (1972) Atmospheric dimethyl sulphide and the natural sulphur cycle. Nature 237: 452-453.
    • (1972) Nature , vol.237 , pp. 452-453
    • Lovelock, J.E.1    Maggs, R.J.2    Rasmussen, R.A.3
  • 30
    • 35148888991 scopus 로고    scopus 로고
    • Transcriptional response of Silicibacter pomeroyi DSS-3 to dimethylsulfoniopropionate (DMSP)
    • Bürgmann H, Howard EC, Ye W, Sun F, Sun S, et al. (2007) Transcriptional response of Silicibacter pomeroyi DSS-3 to dimethylsulfoniopropionate (DMSP). Environ Microbiol 9: 2742-2755.
    • (2007) Environ Microbiol , vol.9 , pp. 2742-2755
    • Bürgmann, H.1    Howard, E.C.2    Ye, W.3    Sun, F.4    Sun, S.5
  • 31
    • 13444263419 scopus 로고    scopus 로고
    • Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum
    • Herrmann G, Selmer T, Jessen HJ, Gokarn RR, Selifonova O, et al. (2005) Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum. FEBS J 272: 813-821.
    • (2005) FEBS J , vol.272 , pp. 813-821
    • Herrmann, G.1    Selmer, T.2    Jessen, H.J.3    Gokarn, R.R.4    Selifonova, O.5
  • 32
    • 0022361252 scopus 로고
    • The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct
    • Shaw L, Engel PC, (1985) The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct. Biochem J 230: 723-731.
    • (1985) Biochem J , vol.230 , pp. 723-731
    • Shaw, L.1    Engel, P.C.2
  • 33
    • 0036282337 scopus 로고    scopus 로고
    • The enigmatic Escherichia coli fadE Gene Is yafH
    • Campbell JW, Cronan JE Jr, (2002) The enigmatic Escherichia coli fadE Gene Is yafH. J Bact 184: 3759-3764.
    • (2002) J Bact , vol.184 , pp. 3759-3764
    • Campbell, J.W.1    Cronan Jr., J.E.2
  • 34
    • 0023664486 scopus 로고
    • Substrate specificity of acetyl coenzyme A synthetase
    • Patel SS, Walt DR, (1987) Substrate specificity of acetyl coenzyme A synthetase. J Biol Chem 262: 7132-7134.
    • (1987) J Biol Chem , vol.262 , pp. 7132-7134
    • Patel, S.S.1    Walt, D.R.2
  • 35
    • 77649185244 scopus 로고    scopus 로고
    • Do the organic sulfur compounds DMSP and DMS drive coral microbial associations?
    • Raina JB, Dinsdale EA, Willis BL, Bourne DG, (2010) Do the organic sulfur compounds DMSP and DMS drive coral microbial associations? Trends Microbiol 18: 101-108.
    • (2010) Trends Microbiol , vol.18 , pp. 101-108
    • Raina, J.B.1    Dinsdale, E.A.2    Willis, B.L.3    Bourne, D.G.4
  • 36
    • 77954861826 scopus 로고    scopus 로고
    • High levels of acrylate in the Great Barrier Reef coral Acropora millepora
    • Tapiolas DM, Motti CA, Holloway P, Boyle SG, (2010) High levels of acrylate in the Great Barrier Reef coral Acropora millepora. Coral Reefs 29: 621-625.
    • (2010) Coral Reefs , vol.29 , pp. 621-625
    • Tapiolas, D.M.1    Motti, C.A.2    Holloway, P.3    Boyle, S.G.4
  • 37
    • 43949120140 scopus 로고    scopus 로고
    • Diversity, ecology, and genomics of the Roseobacter clade: a short overview
    • Brinkhoff T, Giebel H-A, Simon M, (2008) Diversity, ecology, and genomics of the Roseobacter clade: a short overview. Arch Microbiol 189: 531-539.
    • (2008) Arch Microbiol , vol.189 , pp. 531-539
    • Brinkhoff, T.1    Giebel, H.-A.2    Simon, M.3
  • 38
    • 0030222847 scopus 로고    scopus 로고
    • Production of methanethiol from dimethylsulfoniopropionate in marine surface waters
    • Kiene RP, (1996) Production of methanethiol from dimethylsulfoniopropionate in marine surface waters. Mar Chem 54: 69-83.
    • (1996) Mar Chem , vol.54 , pp. 69-83
    • Kiene, R.P.1
  • 39
    • 0025747998 scopus 로고
    • New routes for aerobic biodegradation of dimethylsulfoniopropionate
    • Taylor BF, Gilchrist DC, (1991) New routes for aerobic biodegradation of dimethylsulfoniopropionate. Appl Environ Microbiol 57: 3581-3584.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 3581-3584
    • Taylor, B.F.1    Gilchrist, D.C.2
  • 40
    • 0037338481 scopus 로고    scopus 로고
    • Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein
    • Hetzel M, Brock M, Selmer T, Pierik AJ, Golding BT, et al. (2003) Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein. Eur J Biochem 270: 902-910.
    • (2003) Eur J Biochem , vol.270 , pp. 902-910
    • Hetzel, M.1    Brock, M.2    Selmer, T.3    Pierik, A.J.4    Golding, B.T.5
  • 41
    • 67650302869 scopus 로고    scopus 로고
    • 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales
    • Teufel R, Kung JW, Kockelkorn D, Alber BE, Fuchs G, (2009) 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J Bacteriol 191: 4572-4581.
    • (2009) J Bacteriol , vol.191 , pp. 4572-4581
    • Teufel, R.1    Kung, J.W.2    Kockelkorn, D.3    Alber, B.E.4    Fuchs, G.5
  • 42
    • 0037023756 scopus 로고    scopus 로고
    • Propionyl-coenzyme A synthase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation
    • Alber BE, Fuchs G, (2002) Propionyl-coenzyme A synthase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. J Biol Chem 277: 12137-12143.
    • (2002) J Biol Chem , vol.277 , pp. 12137-12143
    • Alber, B.E.1    Fuchs, G.2
  • 44
    • 0141837820 scopus 로고    scopus 로고
    • Silicibacter pomeroyi sp. nov. and Roseovarius nubinhibens sp. nov., dimethylsulfoniopropionate-demethylating bacteria from marine environments
    • Gonzalez JM, Covert JS, Whitman WB, Henriksen JR, Mayer F, et al. (2003) Silicibacter pomeroyi sp. nov. and Roseovarius nubinhibens sp. nov., dimethylsulfoniopropionate-demethylating bacteria from marine environments. Int J Syst Evol Microbiol 53: 1261-1269.
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 1261-1269
    • Gonzalez, J.M.1    Covert, J.S.2    Whitman, W.B.3    Henriksen, J.R.4    Mayer, F.5
  • 45
    • 0030788037 scopus 로고    scopus 로고
    • Sagittula stellata gen. nov., sp. nov., a lignin-transforming bacterium from a coastal environment
    • Gonzalez JM, Mayer F, Moran MA, Hodson RE, Whitman WB, (1997) Sagittula stellata gen. nov., sp. nov., a lignin-transforming bacterium from a coastal environment. Int J Syst Bacteriol 47: 773-780.
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 773-780
    • Gonzalez, J.M.1    Mayer, F.2    Moran, M.A.3    Hodson, R.E.4    Whitman, W.B.5
  • 46
    • 0000474765 scopus 로고
    • The nodD gene of Rhizobium leguminosarum is autoregulatory and in the presence of plant exudate induces the nodA,B,C genes
    • Rossen L, Shearman CA, Johnston AW, Downie JA, (1985) The nodD gene of Rhizobium leguminosarum is autoregulatory and in the presence of plant exudate induces the nodA,B,C genes. EMBO J 4: 3369-3373.
    • (1985) EMBO J , vol.4 , pp. 3369-3373
    • Rossen, L.1    Shearman, C.A.2    Johnston, A.W.3    Downie, J.A.4
  • 48
    • 0035725442 scopus 로고    scopus 로고
    • The Rhizobium leguminosarum tonB gene is required for the uptake of siderophore and haem as sources of iron
    • Wexler M, Yeoman KH, Stevens JB, de Luca NG, Sawers G, et al. (2001) The Rhizobium leguminosarum tonB gene is required for the uptake of siderophore and haem as sources of iron. Mol Microbiol 41: 801-816.
    • (2001) Mol Microbiol , vol.41 , pp. 801-816
    • Wexler, M.1    Yeoman, K.H.2    Stevens, J.B.3    de Luca, N.G.4    Sawers, G.5
  • 49
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski DH, Helinski DR, (1979) Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci U S A 76: 1648-1652.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 50
    • 0003057316 scopus 로고
    • The culture, general physiology, morphology, and classification of the non-sulfur purple and brown bacteria
    • van Niel CB, (1944) The culture, general physiology, morphology, and classification of the non-sulfur purple and brown bacteria. Bact Rev 8: 1-118.
    • (1944) Bact Rev , vol.8 , pp. 1-118
    • van Niel, C.B.1
  • 52
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria
    • Keen NT, Tamaki S, Kobayashi D, Trollinger D, (1988) Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70: 191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 53
    • 0013889292 scopus 로고
    • Host specificity of DNA produced by Escherichia coli: bacterial mutations affecting the restriction and modification of DNA
    • Wood WB, (1966) Host specificity of DNA produced by Escherichia coli: bacterial mutations affecting the restriction and modification of DNA. J Mol Biol 16: 118-133.
    • (1966) J Mol Biol , vol.16 , pp. 118-133
    • Wood, W.B.1
  • 55
    • 0023506006 scopus 로고
    • Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea
    • Staskawicz B, Dahlbeck D, Keen N, Napoli C, (1987) Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea. J Bacteriol 169: 5789-5794.
    • (1987) J Bacteriol , vol.169 , pp. 5789-5794
    • Staskawicz, B.1    Dahlbeck, D.2    Keen, N.3    Napoli, C.4
  • 56
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schafer A, Tauch A, Jager W, Kalinowski J, Thierbach G, et al. (1994) Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145: 69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schafer, A.1    Tauch, A.2    Jager, W.3    Kalinowski, J.4    Thierbach, G.5
  • 57
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2.
    • (2006) Mol Syst Biol , vol.2
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5
  • 58
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM, (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 59
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S, (2011) MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6


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