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Volumn 194, Issue 10, 2012, Pages 2703-2714

Genetic control of osmoadaptive glycine betaine synthesis in Bacillus subtilis through the choline-sensing and glycine betaine-responsive GbsR repressor

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BACTERIAL ENZYME; BETAINE; CHOLINE; GBSA ENZYME; GBSAB ENZYME; GBSB ENZYME; GBSR PROTEIN; OPUB PROTEIN; OPUC PROTEIN; REGULATOR PROTEIN; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84861365298     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06642-11     Document Type: Article
Times cited : (48)

References (65)
  • 1
    • 80053577856 scopus 로고    scopus 로고
    • Choline uptake in Agrobacterium tumefaciens by the high-affinity ChoXWV transporter
    • Aktas M, Jost KA, Fritz C, Narberhaus F. 2011. Choline uptake in Agrobacterium tumefaciens by the high-affinity ChoXWV transporter. J. Bacteriol. 193:5119-5129.
    • (2011) J. Bacteriol. , vol.193 , pp. 5119-5129
    • Aktas, M.1    Jost, K.A.2    Fritz, C.3    Narberhaus, F.4
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T. 2006. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0028106108 scopus 로고
    • Osmoregulation in Bacillus subtilis: synthesis of the osmoprotectant glycine betaine from exogenously provided choline
    • Boch J, Kempf B, Bremer E. 1994. Osmoregulation in Bacillus subtilis: synthesis of the osmoprotectant glycine betaine from exogenously provided choline. J. Bacteriol. 176:5364-5371.
    • (1994) J. Bacteriol. , vol.176 , pp. 5364-5371
    • Boch, J.1    Kempf, B.2    Bremer, E.3
  • 5
    • 0029788980 scopus 로고    scopus 로고
    • Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis: characterization of the gbsAB genes
    • Boch J, Kempf B, Schmid R, Bremer E. 1996. Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis: characterization of the gbsAB genes. J. Bacteriol. 178:5121-5129.
    • (1996) J. Bacteriol , vol.178 , pp. 5121-5129
    • Boch, J.1    Kempf, B.2    Schmid, R.3    Bremer, E.4
  • 6
    • 0030763455 scopus 로고    scopus 로고
    • Glycine betaine aldehyde dehydrogenase from Bacillus subtilis: characterization of an enzyme required for the synthesis of the osmoprotectant glycine betaine
    • Boch J, Nau-Wagner G, Kneip S, Bremer E. 1997. Glycine betaine aldehyde dehydrogenase from Bacillus subtilis: characterization of an enzyme required for the synthesis of the osmoprotectant glycine betaine. Arch. Microbiol. 168:282-289.
    • (1997) Arch. Microbiol. , vol.168 , pp. 282-289
    • Boch, J.1    Nau-Wagner, G.2    Kneip, S.3    Bremer, E.4
  • 7
    • 79952923961 scopus 로고    scopus 로고
    • Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1
    • Borwankar T, et al. 2011. Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1. Biochemistry 50:2048-2060.
    • (2011) Biochemistry , vol.50 , pp. 2048-2060
    • Borwankar, T.1
  • 8
    • 0033966210 scopus 로고    scopus 로고
    • Glycine betaine-assisted protein folding in a lysA mutant of Escherichia coli
    • Bourot S, et al. 2000. Glycine betaine-assisted protein folding in a lysA mutant of Escherichia coli. J. Biol. Chem. 275:1050-1056.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1050-1056
    • Bourot, S.1
  • 9
    • 0013164730 scopus 로고    scopus 로고
    • Adaptation to changing osmolarity
    • (ed), Bacillus subtilis and its closest relatives ASM Press, Washington, DC
    • Bremer E. 2002. Adaptation to changing osmolarity, p 385-391. In Sonenshein AL, Hoch JA, Losick R (ed), Bacillus subtilis and its closest relatives. ASM Press, Washington, DC.
    • (2002) Sonenshein AL, Hoch JA, Losick R , pp. 385-391
    • Bremer, E.1
  • 10
    • 84861415716 scopus 로고    scopus 로고
    • A look into the aromatic cage
    • Bremer E. 2011. A look into the aromatic cage. Environ. Microbiol. Rep. 3:1-5.
    • (2011) Environ. Microbiol. Re , vol.3 , pp. 1-5
    • Bremer, E.1
  • 11
    • 0002619615 scopus 로고    scopus 로고
    • Coping with osmotic challenges: osmoregulation through accumulation and release of compatible solutes
    • In Storz G, Hengge-Aronis R .(ed)ASM Press, Washington, DC
    • Bremer E, Krämer R. 2000. Coping with osmotic challenges: osmoregulation through accumulation and release of compatible solutes, p 79-97. In Storz G, Hengge-Aronis R (ed), Bacterial stress responses..
    • (2000) Bacterial stress responses , pp. 79-97
    • Bremer, E.1    Krämer, R.2
  • 12
    • 0038444555 scopus 로고    scopus 로고
    • Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to low-temperature adaptation
    • Brigulla M, et al. 2003. Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to low-temperature adaptation. J. Bacteriol. 185:4305-4514.
    • (2003) J. Bacteriol , vol.185 , pp. 4305-4514
    • Brigulla, M.1
  • 13
    • 80053613797 scopus 로고    scopus 로고
    • Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity
    • Brill J, Hoffmann T, Bleisteiner M, Bremer E. 2011. Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity. J. Bacteriol. 193:5335-5346.
    • (2011) J. Bacteriol. , vol.193 , pp. 5335-5346
    • Brill, J.1    Hoffmann, T.2    Bleisteiner, M.3    Bremer, E.4
  • 14
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii
    • Bult CJ, et al. 1996. Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii. Science 273:1058-1073.
    • (1996) Science , pp. 1058-1073
    • Bult, C.J.1
  • 15
    • 77955321729 scopus 로고    scopus 로고
    • Synthesis of glycine betaine from choline in the moderate halophile Halobacillus halophilus: co-regulation of two divergent, polycistronic operons
    • Burkhardt J, Sewald X, Bauer B, Saum SH, Müller V. 2009. Synthesis of glycine betaine from choline in the moderate halophile Halobacillus halophilus: co-regulation of two divergent, polycistronic operons. Environ. Microbiol. Rep. 1:38-43.
    • (2009) Environ. Microbiol. Re , vol.1 , pp. 38-43
    • Burkhardt, J.1    Sewald, X.2    Bauer, B.3    Saum, S.H.4    Müller, V.5
  • 16
    • 9244263009 scopus 로고    scopus 로고
    • The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42°C
    • Chattopadhyay MK, et al. 2004. The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42°C. J. Bacteriol. 186:8149-8152.
    • (2004) J. Bacteriol. , vol.186 , pp. 8149-8152
    • Chattopadhyay, M.K.1
  • 17
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant S, Eliahu N, Rosenthal D, Goloubinoff P. 2001. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 276:39586-39591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 18
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • Dougherty DA. 1996. Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271:163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 19
    • 79956015881 scopus 로고    scopus 로고
    • Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC
    • Du Y, et al. 2011. Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC. Biochem. J. 436:283-289.
    • (2011) Biochem. J. , vol.436 , pp. 283-289
    • Du, Y.1
  • 21
    • 0029873989 scopus 로고    scopus 로고
    • Glycine betaine fluxes in Lactobacillus plantarum during osmostasis and hyper- and hypo-osmotic shock
    • Glaasker E, Konings WN, Poolman B. 1996. Glycine betaine fluxes in Lactobacillus plantarum during osmostasis and hyper- and hypo-osmotic shock. J. Biol. Chem. 271:10060-10065.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10060-10065
    • Glaasker, E.1    Konings, W.N.2    Poolman, B.3
  • 23
    • 50249084952 scopus 로고    scopus 로고
    • Characterization of the glycine betaine biosynthetic genes in the moderately halophilic bacterium Halobacillus dabanensis D-8T
    • Gu ZJ, Wang L, Le Rudulier D, Zhang B, Yang SS. 2008. Characterization of the glycine betaine biosynthetic genes in the moderately halophilic bacterium Halobacillus dabanensis D-8T. Curr. Microbiol. 57:306-311.
    • (2008) Curr. Microbiol. , vol.57 , pp. 306-311
    • Gu, Z.J.1    Wang, L.2    Le Rudulier, D.3    Zhang, B.4    Yang, S.5
  • 24
    • 75149171079 scopus 로고    scopus 로고
    • A comprehensive proteomics and transcriptomics analysis of Bacillus subtilis salt stress adaptation
    • Hahne H, et al. 2010. A comprehensive proteomics and transcriptomics analysis of Bacillus subtilis salt stress adaptation. J. Bacteriol. 192:870-882.
    • (2010) J. Bacteriol. , vol.192 , pp. 870-882
    • Hahne, H.1
  • 25
    • 0002201126 scopus 로고
    • Growth, maintenance and general techniques In Harwood CR, Cutting SM (ed), Molecular biological methods for Bacillus. John Wiley & Sons, Chichester
    • Harwood CR, Archibald AR. 1990. Growth, maintenance and general techniques, p 1-26. In Harwood CR, Cutting SM (ed), Molecular biological methods for Bacillus. John Wiley & Sons, Chichester, United Kingdom.
    • (1990) United Kingdom , pp. 1-26
    • Harwood, C.R.1    Archibald, A.R.2
  • 26
    • 0003492044 scopus 로고
    • Molecular biological methods for Bacillus
    • Chichester, United Kingdom
    • Harwood CR, Cutting SM. 1990. Molecular biological methods for Bacillus. John Wiley & Sons, Chichester, United Kingdom.
    • (1990) John Wiley & Sons
    • Harwood, C.R.1    Cutting, S.M.2
  • 28
    • 0029041524 scopus 로고
    • Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter
    • Helmann JD. 1995. Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA. Nucleic Acids Res. 23: 2351-2360.
    • (1995) DNA. Nucleic Acids Res , vol.23 , pp. 2351-2360
    • Helmann, J.D.1
  • 29
    • 42349084634 scopus 로고    scopus 로고
    • Responses of Bacillus subtilis to hypotonic challenges: physiological contributions of mechanosensitive channels to cellular survival
    • Hoffmann T, Boiangiu C, Moses S, Bremer E. 2008. Responses of Bacillus subtilis to hypotonic challenges: physiological contributions of mechanosensitive channels to cellular survival. Appl. Environ. Microbiol. 74:2454-2460.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 2454-2460
    • Hoffmann, T.1    Boiangiu, C.2    Moses, S.3    Bremer, E.4
  • 30
    • 79952794459 scopus 로고    scopus 로고
    • Protection of Bacillus subtilis against cold stress via compatible-solute acquisition
    • Hoffmann T, Bremer E. 2011. Protection of Bacillus subtilis against cold stress via compatible-solute acquisition. J. Bacteriol. 193:1552-1562.
    • (2011) J. Bacteriol , vol.193 , pp. 1552-1562
    • Hoffmann, T.1    Bremer, E.2
  • 31
    • 1542376971 scopus 로고    scopus 로고
    • Thermoprotection of Bacillus subtilis by exogenously provided glycine betaine and structurally related compatible solutes: involvement of Opu transporters
    • Holtmann G, Bremer E. 2004. Thermoprotection of Bacillus subtilis by exogenously provided glycine betaine and structurally related compatible solutes: involvement of Opu transporters. J. Bacteriol. 186:1683-1693.
    • (2004) J. Bacteriol. , vol.186 , pp. 1683-1693
    • Holtmann, G.1    Bremer, E.2
  • 32
    • 33344456354 scopus 로고    scopus 로고
    • Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine
    • Horn C, et al. 2006. Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine. J. Mol. Biol. 357:592-606.
    • (2006) J. Mol. Biol. , vol.357 , pp. 592-606
    • Horn, C.1
  • 33
    • 0036468362 scopus 로고    scopus 로고
    • Prokaryotic transcription regulators: more than just the helix-turn-helix motif
    • Huffman JL, Brennan RG. 2002. Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol. 12:98-106.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 98-106
    • Huffman, J.L.1    Brennan, R.G.2
  • 34
    • 0031963131 scopus 로고    scopus 로고
    • Response of Bacillus subtilis to high osmolarity: uptake of carnitine, crotonobetaine and butyrobetaine via the ABC transport system OpuC
    • Kappes RM, Bremer E. 1998. Response of Bacillus subtilis to high osmolarity: uptake of carnitine, crotonobetaine and butyrobetaine via the ABC transport system OpuC. Microbiology 144:83-90.
    • (1998) Microbiology , vol.144 , pp. 83-90
    • Kappes, R.M.1    Bremer, E.2
  • 35
    • 0029812908 scopus 로고    scopus 로고
    • Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD
    • Kappes RM, Kempf B, Bremer E. 1996. Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD. J. Bacteriol. 178:5071-5079.
    • (1996) J. Bacteriol. , vol.178 , pp. 5071-5079
    • Kappes, R.M.1    Kempf, B.2    Bremer, E.3
  • 36
    • 0032940227 scopus 로고    scopus 로고
    • Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis
    • Kappes RM, et al. 1999. Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis. Mol. Microbiol. 32:203-216.
    • (1999) Mol. Microbiol. , pp. 203-216
    • Kappes, R.M.1
  • 37
    • 0029025354 scopus 로고
    • OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis
    • Kempf B, Bremer E. 1995. OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J. Biol. Chem. 270:16701-16713.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16701-16713
    • Kempf, B.1    Bremer, E.2
  • 38
    • 0031719418 scopus 로고    scopus 로고
    • Uptake and synthesis of compatible solutes as microbial stress responses to high osmolality environments
    • Kempf B, Bremer E. 1998. Uptake and synthesis of compatible solutes as microbial stress responses to high osmolality environments. Arch. Microbiol. 170:319-330.
    • (1998) Arch. Microbiol. , vol.170 , pp. 319-330
    • Kempf, B.1    Bremer, E.2
  • 39
    • 77749254876 scopus 로고    scopus 로고
    • Glycine betaine biosynthesized from glycine provides an osmolyte for cell growth and spore germination during osmotic stress in Myxococcus xanthus
    • Kimura Y, Kawasaki S, Yoshimoto H, Takegawa K. 2010. Glycine betaine biosynthesized from glycine provides an osmolyte for cell growth and spore germination during osmotic stress in Myxococcus xanthus. J. Bacteriol. 192:1467-1470.
    • (2010) J. Bacteriol. , vol.192 , pp. 1467-1470
    • Kimura, Y.1    Kawasaki, S.2    Yoshimoto, H.3    Takegawa, K.4
  • 40
    • 0026040666 scopus 로고
    • Regulation of compatible solute accumulation in Salmonella typhimurium: evidence for a glycine betaine efflux system
    • Koo SP, Higgins CF, Booth IR. 1991. Regulation of compatible solute accumulation in Salmonella typhimurium: evidence for a glycine betaine efflux system. J. Gen. Microbiol. 137:2617-2625.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2617-2625
    • Koo, S.P.1    Higgins, C.F.2    Booth, I.R.3
  • 41
    • 0014723017 scopus 로고
    • The aerobic decomposition of choline by microorganisms
    • Kortstee GJ. 1970. The aerobic decomposition of choline by microorganisms. Arch. Microbiol. 71:235-244.
    • (1970) Arch. Microbiol. , vol.71 , pp. 235-244
    • Kortstee, G.J.1
  • 42
    • 0025736051 scopus 로고
    • DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli
    • Lamark T, et al. 1991. DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli. Mol. Microbiol. 5:1049-1064.
    • (1991) Mol. Microbiol , vol.5 , pp. 1049-1064
    • Lamark, T.1
  • 43
    • 0027120895 scopus 로고
    • Efflux of choline and glycine betaine from osmoregulating cells of Escherichia coli
    • Lamark T, Styrvold OB, Strom AR. 1992. Efflux of choline and glycine betaine from osmoregulating cells of Escherichia coli. FEMS Microbiol. Lett. 75:149-154.
    • (1992) FEMS Microbiol. Lett. , vol.75 , pp. 149-154
    • Lamark, T.1    Styrvold, O.B.2    Strom, A.R.3
  • 45
    • 0033013656 scopus 로고    scopus 로고
    • High-affinity transport of choline-O-sulfate and its use as a compatible solute in Bacillus subtilis
    • Nau-Wagner G, Boch J, Le Good JA, Bremer E. 1999. High-affinity transport of choline-O-sulfate and its use as a compatible solute in Bacillus subtilis. Appl. Environ. Microbiol. 65:560-568.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 560-568
    • Nau-Wagner, G.1    Boch, J.2    Le Good, J.3    Bremer, E.4
  • 47
    • 57749122030 scopus 로고    scopus 로고
    • Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states
    • Oswald C, et al. 2008. Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states. J. Biol. Chem. 283:32848-32859.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32848-32859
    • Oswald, C.1
  • 48
    • 79960698795 scopus 로고    scopus 로고
    • The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline
    • Pittelkow M, Tschapek B, Smits SH, Schmitt L, Bremer E. 2011. The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline. J. Mol. Biol. 411:53-67.
    • (2011) J. Mol. Biol , vol.411 , pp. 53-67
    • Pittelkow, M.1    Tschapek, B.2    Smits, S.H.3    Schmitt, L.4    Bremer, E.5
  • 49
    • 67650541861 scopus 로고    scopus 로고
    • Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase
    • Quaye O, Cowins S, Gadda G. 2009. Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase. J. Biol. Chem. 284:16990-16997.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16990-16997
    • Quaye, O.1    Cowins, S.2    Gadda, G.3
  • 50
    • 0037233841 scopus 로고    scopus 로고
    • X- ray structure of an M. jannaschii DNA-binding protein: implications for antibiotic resistance in S. aureus
    • Ray SS, et al. 2003. X-ray structure of an M. jannaschii DNA-binding protein: implications for antibiotic resistance in S. aureus. Proteins 50: 170-173.
    • (2003) Proteins , vol.50 , pp. 170-173
    • Ray, S.S.1
  • 51
    • 0032936309 scopus 로고    scopus 로고
    • The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization
    • Rosenstein R, Futter-Bryniok D, Götz F. 1999. The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. J. Bacteriol. 181:2273-2278.
    • (1999) J. Bacteriol. , vol.181 , pp. 2273-2278
    • Rosenstein, R.1    Futter-Bryniok, D.2    Götz, F.3
  • 52
    • 1242339645 scopus 로고    scopus 로고
    • Cation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli
    • Schiefner A, et al. 2004. Cation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli. J. Biol. Chem. 279:5588-5596.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5588-5596
    • Schiefner, A.1
  • 53
    • 49449086824 scopus 로고    scopus 로고
    • The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies
    • Smits SH, et al. 2008. The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies. J. Bacteriol. 190:5663-5671.
    • (2008) J. Bacteriol. , vol.190 , pp. 5663-5671
    • Smits, S.H.1
  • 54
    • 50849126804 scopus 로고    scopus 로고
    • High-precision, whole-genome sequencing of laboratory strains facilitates genetic studies
    • Srivatsan A, et al. 2008. High-precision, whole-genome sequencing of laboratory strains facilitates genetic studies. PLoS Genet. 4:e1000139.
    • (2008) PLoS Genet , vol.4
    • Srivatsan, A.1
  • 55
    • 0142214662 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling analysis of adaptation of Bacillus subtilis to high salinity
    • Steil L, Hoffmann T, Budde I, Völker U, Bremer E. 2003. Genome-wide transcriptional profiling analysis of adaptation of Bacillus subtilis to high salinity. J. Bacteriol. 185:6358-6370.
    • (2003) J. Bacteriol. , vol.185 , pp. 6358-6370
    • Steil, L.1    Hoffmann, T.2    Budde, I.3    Völker, U.4    Bremer, E.5
  • 57
    • 0034255358 scopus 로고    scopus 로고
    • DbClustal: rapid and reliable global multiple alignments of protein sequences detected by database searches
    • Thompson JD, Plewniak F, Thierry JC, Poch O. 2000. DbClustal: rapid and reliable global multiple alignments of protein sequences detected by database searches. Nucleic Acids Res. 28:2919-2926.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2919-2926
    • Thompson, J.D.1    Plewniak, F.2    Thierry, J.C.3    Poch, O.4
  • 58
    • 79960697231 scopus 로고    scopus 로고
    • Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state
    • Tschapek B, et al. 2011. Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state. J. Mol. Biol. 411:36-52.
    • (2011) J. Mol. Biol. , vol.411 , pp. 36-52
    • Tschapek, B.1
  • 59
    • 13444267296 scopus 로고    scopus 로고
    • Genes for direct methylation of glycine provide high levels of glycinebetaine and abiotic-stress tolerance in Synechococcus and Arabidopsis
    • Waditee R, et al. 2005. Genes for direct methylation of glycine provide high levels of glycinebetaine and abiotic-stress tolerance in Synechococcus and Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 102:1318-1323.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 1318-1323
    • Waditee, R.1
  • 60
    • 67349152920 scopus 로고    scopus 로고
    • Levels and localization of mechanosensitive channel proteins in Bacillus subtilis
    • Wahome PG, Cowan AE, Setlow B, Setlow P. 2009. Levels and localization of mechanosensitive channel proteins in Bacillus subtilis. Arch. Microbiol. 191:403-414.
    • (2009) Arch. Microbiol. , vol.191 , pp. 403-414
    • Wahome, P.G.1    Cowan, A.E.2    Setlow, B.3    Setlow, P.4
  • 61
    • 0025674148 scopus 로고
    • The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis
    • Whatmore AM, Chudek JA, Reed RH. 1990. The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis. J. Gen. Microbiol. 136:2527-2535.
    • (1990) J. Gen. Microbiol , vol.136 , pp. 2527-2535
    • Whatmore, A.M.1    Chudek, J.A.2    Reed, R.H.3
  • 63
    • 0034794118 scopus 로고    scopus 로고
    • Osmosensing and osmoregulatory compatible solute accumulation by bacteria
    • Wood JM, et al. 2001. Osmosensing and osmoregulatory compatible solute accumulation by bacteria. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 130:437-460.
    • (2001) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.130 , pp. 437-460
    • Wood, J.M.1
  • 64
    • 24644450812 scopus 로고    scopus 로고
    • Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses
    • Yancey PH. 2005. Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses. J. Exp. Biol. 208:2819-2830.
    • (2005) J. Exp. Biol. , vol.208 , pp. 2819-2830
    • Yancey, P.H.1
  • 65
    • 77957234040 scopus 로고    scopus 로고
    • The BCCT family of carriers: from physiology to crystal structure
    • Ziegler C, Bremer E, Krämer R. 2010. The BCCT family of carriers: from physiology to crystal structure. Mol. Microbiol. 78:13-34.
    • (2010) Mol. Microbiol. , vol.78 , pp. 13-34
    • Ziegler, C.1    Bremer, E.2    Krämer, R.3


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