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Volumn 158, Issue 2, 2012, Pages 368-379

Role of a short light, oxygen, voltage (LOV) domain protein in blue light-and singlet oxygen-dependent gene regulation in Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; LIGHT OXYGEN VOLTAGE DOMAIN PROTEIN; TRANSCRIPTOME; UNCLASSIFIED DRUG;

EID: 84856948684     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.054700-0     Document Type: Article
Times cited : (25)

References (68)
  • 1
    • 18144373854 scopus 로고    scopus 로고
    • A transcriptional response to singlet oxygen, a toxic byproduct of photosynthesis
    • Anthony, J. R., Warczak, K. L. & Donohue, T. J. (2005). A transcriptional response to singlet oxygen, a toxic byproduct of photosynthesis. Proc Natl Acad Sci U S A 102, 6502-6507
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6502-6507
    • Anthony, J.R.1    Warczak, K.L.2    Donohue, T.J.3
  • 2
    • 0033953284 scopus 로고    scopus 로고
    • The STAS domain-a link between anion transporters and antisigma-factor antagonists
    • Aravind, L. & Koonin, E. V. (2000). The STAS domain-a link between anion transporters and antisigma-factor antagonists. Curr Biol 10, R53-R55.
    • (2000) Curr Biol , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 33749021097 scopus 로고    scopus 로고
    • Blue light activates the s-dependent stress response of Bacillus subtilis via YtvA
    • Avila-Pérez, M., Hellingwerf, K. J. & Kort, R. (2006). Blue light activates the s-dependent stress response of Bacillus subtilis via YtvA. J Bacteriol 188, 6411-6414
    • (2006) J Bacteriol , vol.188 , pp. 6411-6414
    • Avila-Pérez, M.1    Hellingwerf, K.J.2    Kort, R.3
  • 4
    • 69949148703 scopus 로고    scopus 로고
    • In vivo mutational analysis of YtvA from Bacillus subtilis: Mechanism of light activation of the general stress response
    • Avila-Pérez, M., Vreede, J., Tang, Y., Bende, O., Losi, A., Gärtner, W. & Hellingwerf, K. J. (2009). In vivo mutational analysis of YtvA from Bacillus subtilis: mechanism of light activation of the general stress response. J Biol Chem 284, 24958-24964
    • (2009) J Biol Chem , vol.284 , pp. 24958-24964
    • Avila-Pérez, M.1    Vreede, J.2    Tang, Y.3    Bende, O.4    Losi, A.5    Gärtner, W.6    Hellingwerf, K.J.7
  • 5
    • 0031929614 scopus 로고    scopus 로고
    • The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium
    • Beck, B. J. & Downs, D. M. (1998). The apbE gene encodes a lipoprotein involved in thiamine synthesis in Salmonella typhimurium. J Bacteriol 180, 885-891
    • (1998) J Bacteriol , vol.180 , pp. 885-891
    • Beck, B.J.1    Downs, D.M.2
  • 6
    • 0033984378 scopus 로고    scopus 로고
    • Identification of the operon for the sorbitol (glucitol) phosphoenolpyruvate: Sugar phosphotransferase system in Streptococcus mutans
    • Boyd, D. A., Thevenot, T., Gumbmann, M., Honeyman, A. L. & Hamilton, I. R. (2000). Identification of the operon for the sorbitol (glucitol) phosphoenolpyruvate: sugar phosphotransferase system in Streptococcus mutans. Infect Immun 68, 925-930
    • (2000) Infect Immun , vol.68 , pp. 925-930
    • Boyd, D.A.1    Thevenot, T.2    Gumbmann, M.3    Honeyman, A.L.4    Hamilton, I.R.5
  • 7
    • 0442314286 scopus 로고    scopus 로고
    • Blue light perception in bacteria
    • Braatsch, S. & Klug, G. (2004). Blue light perception in bacteria. Photosynth Res 79, 45-57
    • (2004) Photosynth Res , vol.79 , pp. 45-57
    • Braatsch, S.1    Klug, G.2
  • 8
    • 0036371637 scopus 로고    scopus 로고
    • A single flavoprotein, AppA, integrates both redox and light signals in Rhodobacter sphaeroides
    • Braatsch, S., Gomelsky, M., Kuphal, S. & Klug, G. (2002). A single flavoprotein, AppA, integrates both redox and light signals in Rhodobacter sphaeroides. Mol Microbiol 45, 827-836
    • (2002) Mol Microbiol , vol.45 , pp. 827-836
    • Braatsch, S.1    Gomelsky, M.2    Kuphal, S.3    Klug, G.4
  • 9
    • 34447316738 scopus 로고    scopus 로고
    • The LOV domain: A chromophore module servicing multiple photoreceptors
    • Briggs, W. R. (2007). The LOV domain: a chromophore module servicing multiple photoreceptors. J Biomed Sci 14, 499-504
    • (2007) J Biomed Sci , vol.14 , pp. 499-504
    • Briggs, W.R.1
  • 10
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • Briggs, W. R. & Christie, J. M. (2002). Phototropins 1 and 2: versatile plant blue-light receptors. Trends Plant Sci 7, 204-210
    • (2002) Trends Plant Sci , vol.7 , pp. 204-210
    • Briggs, W.R.1    Christie, J.M.2
  • 11
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • Crosson, S., Rajagopal, S. & Moffat, K. (2003). The LOV domain family: photoresponsive signaling modules coupled to diverse output domains. Biochemistry 42, 2-10
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 12
    • 0026395367 scopus 로고
    • Long-distance deoR regulation of gene expression in Escherichia coli
    • Dandanell, G., Norris, K. & Hammer, K. (1991). Long-distance deoR regulation of gene expression in Escherichia coli. Ann N Y Acad Sci 646, 19-30
    • (1991) Ann N Y Acad Sci , vol.646 , pp. 19-30
    • Dandanell, G.1    Norris, K.2    Hammer, K.3
  • 14
    • 47249107417 scopus 로고    scopus 로고
    • Role of the global transcriptional regulator PrrA in Rhodobacter sphaeroides 2.4.1: Combined transcriptome and proteome analysis
    • Eraso, J. M., Roh, J. H., Zeng, X., Callister, S. J., Lipton, M. S. & Kaplan, S. (2008). Role of the global transcriptional regulator PrrA in Rhodobacter sphaeroides 2.4.1: combined transcriptome and proteome analysis. J Bacteriol 190, 4831-4848
    • (2008) J Bacteriol , vol.190 , pp. 4831-4848
    • Eraso, J.M.1    Roh, J.H.2    Zeng, X.3    Callister, S.J.4    Lipton, M.S.5    Kaplan, S.6
  • 15
    • 21344459291 scopus 로고    scopus 로고
    • Photo-oxidative stress in Rhodobacter sphaeroides: Protective role of carotenoids and expression of selected genes
    • Glaeser, J. & Klug, G. (2005). Photo-oxidative stress in Rhodobacter sphaeroides: protective role of carotenoids and expression of selected genes. Microbiology 151, 1927-1938
    • (2005) Microbiology , vol.151 , pp. 1927-1938
    • Glaeser, J.1    Klug, G.2
  • 16
    • 34547199027 scopus 로고    scopus 로고
    • Protein synthesis patterns reveal a complex regulatory response to singlet oxygen in Rhodobacter
    • Glaeser, J., Zobawa, M., Lottspeich, F. & Klug, G. (2007). Protein synthesis patterns reveal a complex regulatory response to singlet oxygen in Rhodobacter. J Proteome Res 6, 2460-2471
    • (2007) J Proteome Res , vol.6 , pp. 2460-2471
    • Glaeser, J.1    Zobawa, M.2    Lottspeich, F.3    Klug, G.4
  • 17
    • 0029093864 scopus 로고
    • AppA, a novel gene encoding a trans-acting factor involved in the regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1
    • Gomelsky, M. & Kaplan, S. (1995). appA, a novel gene encoding a trans-acting factor involved in the regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J Bacteriol 177, 4609-4618
    • (1995) J Bacteriol , vol.177 , pp. 4609-4618
    • Gomelsky, M.1    Kaplan, S.2
  • 18
    • 0031026315 scopus 로고    scopus 로고
    • Molecular genetic analysis suggesting interactions between AppA and PpsR in regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1
    • Gomelsky, M. & Kaplan, S. (1997). Molecular genetic analysis suggesting interactions between AppA and PpsR in regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J Bacteriol 179, 128-134
    • (1997) J Bacteriol , vol.179 , pp. 128-134
    • Gomelsky, M.1    Kaplan, S.2
  • 19
    • 0036804709 scopus 로고    scopus 로고
    • BLUF: A novel FAD-binding domain involved in sensory transduction in microorganisms
    • Gomelsky, M. & Klug, G. (2002). BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms. Trends Biochem Sci 27, 497-500
    • (2002) Trends Biochem Sci , vol.27 , pp. 497-500
    • Gomelsky, M.1    Klug, G.2
  • 20
    • 0034087474 scopus 로고    scopus 로고
    • Domain structure, oligomeric state, and mutational analysis of PpsR, the Rhodobacter sphaeroides repressor of photosystem gene expression
    • Gomelsky, M., Horne, I. M., Lee, H. J., Pemberton, J. M., McEwan, A. G. & Kaplan, S. (2000). Domain structure, oligomeric state, and mutational analysis of PpsR, the Rhodobacter sphaeroides repressor of photosystem gene expression. J Bacteriol 182, 2253-2261
    • (2000) J Bacteriol , vol.182 , pp. 2253-2261
    • Gomelsky, M.1    Horne, I.M.2    Lee, H.J.3    Pemberton, J.M.4    McEwan, A.G.5    Kaplan, S.6
  • 22
    • 34248328266 scopus 로고    scopus 로고
    • A haem cofactor is required for redox and light signalling by the AppA protein of Rhodobacter sphaeroides
    • Han, Y., Meyer, M. H., Keusgen, M. & Klug, G. (2007). A haem cofactor is required for redox and light signalling by the AppA protein of Rhodobacter sphaeroides. Mol Microbiol 64, 1090-1104
    • (2007) Mol Microbiol , vol.64 , pp. 1090-1104
    • Han, Y.1    Meyer, M.H.2    Keusgen, M.3    Klug, G.4
  • 23
    • 27444435780 scopus 로고    scopus 로고
    • Light-dependent regulation of photosynthesis genes in Rhodobacter sphaeroides 2.4.1 is coordinately controlled by photosynthetic electron transport via the PrrBA two-component system and the photoreceptor AppA
    • Happ, H. N., Braatsch, S., Broschek, V., Osterloh, L. & Klug, G. (2005). Light-dependent regulation of photosynthesis genes in Rhodobacter sphaeroides 2.4.1 is coordinately controlled by photosynthetic electron transport via the PrrBA two-component system and the photoreceptor AppA. Mol Microbiol 58, 903-914
    • (2005) Mol Microbiol , vol.58 , pp. 903-914
    • Happ, H.N.1    Braatsch, S.2    Broschek, V.3    Osterloh, L.4    Klug, G.5
  • 24
    • 0025905579 scopus 로고
    • A new family of bacterial regulatory proteins
    • Haydon, D. J. & Guest, J. R. (1991). A new family of bacterial regulatory proteins. FEMS Microbiol Lett 63, 291-295
    • (1991) FEMS Microbiol Lett , vol.63 , pp. 291-295
    • Haydon, D.J.1    Guest, J.R.2
  • 25
    • 34250697880 scopus 로고    scopus 로고
    • The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a sE-dependent manner
    • Hendrischk, A. K., Braatsch, S., Glaeser, J. & Klug, G. (2007). The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a sE-dependent manner. Microbiology 153, 1842-1851
    • (2007) Microbiology , vol.153 , pp. 1842-1851
    • Hendrischk, A.K.1    Braatsch, S.2    Glaeser, J.3    Klug, G.4
  • 27
    • 69649083589 scopus 로고    scopus 로고
    • Characterization of an unusual LOV domain protein in the aproteobacterium Rhodobacter sphaeroides
    • Hendrischk, A. K., Moldt, J., Frühwirth, S. W. & Klug, G. (2009b). Characterization of an unusual LOV domain protein in the aproteobacterium Rhodobacter sphaeroides. Photochem Photobiol 85, 1254-1259
    • (2009) Photochem Photobiol , vol.85 , pp. 1254-1259
    • Hendrischk, A.K.1    Moldt, J.2    Frühwirth, S.W.3    Klug, G.4
  • 28
    • 0025727991 scopus 로고
    • Expression of regulatory nif genes in Rhodobacter capsulatus
    • Hübner, P., Willison, J. C., Vignais, P. M. & Bickle, T. A. (1991). Expression of regulatory nif genes in Rhodobacter capsulatus. J Bacteriol 173, 2993-2999
    • (1991) J Bacteriol , vol.173 , pp. 2993-2999
    • Hübner, P.1    Willison, J.C.2    Vignais, P.M.3    Bickle, T.A.4
  • 29
    • 0027380393 scopus 로고
    • Nif gene expression studies in Rhodobacter capsulatus: NtrC-independent repression by high ammonium concentrations
    • Hübner, P., Masepohl, B., Klipp, W. & Bickle, T. A. (1993). nif gene expression studies in Rhodobacter capsulatus: ntrC-independent repression by high ammonium concentrations. Mol Microbiol 10, 123-132
    • (1993) Mol Microbiol , vol.10 , pp. 123-132
    • Hübner, P.1    Masepohl, B.2    Klipp, W.3    Bickle, T.A.4
  • 30
    • 29144509559 scopus 로고    scopus 로고
    • The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides
    • Hunter, C. N., Tucker, J. D. & Niederman, R. A. (2005). The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides. Photochem Photobiol Sci 4, 1023-1027
    • (2005) Photochem Photobiol Sci , vol.4 , pp. 1023-1027
    • Hunter, C.N.1    Tucker, J.D.2    Niederman, R.A.3
  • 31
    • 0022599284 scopus 로고
    • Evidence for a coordinate transcriptional control of alpha-toxin and protein-A synthesis in Staphylococcus aureus
    • Janzon, L., Lofdahl, S. & Arvidson, S. (1986). Evidence for a coordinate transcriptional control of alpha-toxin and protein-A synthesis in Staphylococcus aureus. FEMS Microbiol Lett 33, 193-198
    • (1986) FEMS Microbiol Lett , vol.33 , pp. 193-198
    • Janzon, L.1    Lofdahl, S.2    Arvidson, S.3
  • 32
    • 84856957006 scopus 로고    scopus 로고
    • Regulation of genes by light
    • Edited by M. C. Thurnauer. Dordrecht: Springer
    • Klug, G. & Masuda, S. (2009). Regulation of genes by light. In The Purple Phototrophic Bacteria, pp. 727-741. Edited by M. C. Thurnauer. Dordrecht: Springer.
    • (2009) The Purple Phototrophic Bacteria , pp. 727-741
    • Klug, G.1    Masuda, S.2
  • 33
    • 22844446481 scopus 로고    scopus 로고
    • Initial characterization of a blue-light sensing, phototropin-related protein from Pseudomonas putida: A paradigm for an extended LOV construct
    • Krauss, U., Losi, A., Gärtner, W., Jaeger, K. E. & Eggert, T. (2005). Initial characterization of a blue-light sensing, phototropin-related protein from Pseudomonas putida: a paradigm for an extended LOV construct. Phys Chem Chem Phys 7, 2804-2811
    • (2005) Phys Chem Chem Phys , vol.7 , pp. 2804-2811
    • Krauss, U.1    Losi, A.2    Gärtner, W.3    Jaeger, K.E.4    Eggert, T.5
  • 34
    • 36249024090 scopus 로고    scopus 로고
    • Flavin-based blue-light photosensors: A photobiophysics update
    • Losi, A. (2007). Flavin-based blue-light photosensors: a photobiophysics update. Photochem Photobiol 83, 1283-1300
    • (2007) Photochem Photobiol , vol.83 , pp. 1283-1300
    • Losi, A.1
  • 35
    • 53749091743 scopus 로고    scopus 로고
    • Bacterial bilin-and flavin-binding photoreceptors
    • Losi, A. & Gärtner, W. (2008). Bacterial bilin-and flavin-binding photoreceptors. Photochem Photobiol Sci 7, 1168-1178
    • (2008) Photochem Photobiol Sci , vol.7 , pp. 1168-1178
    • Losi, A.1    Gärtner, W.2
  • 36
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • Losi, A., Polverini, E., Quest, B. & Gärtner, W. (2002). First evidence for phototropin-related blue-light receptors in prokaryotes. Biophys J 82, 2627-2634
    • (2002) Biophys J , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gärtner, W.4
  • 37
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • Masuda, S. & Bauer, C. E. (2002). AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. Cell 110, 613-623
    • (2002) Cell , vol.110 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 38
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli sE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
    • Missiakas, D., Mayer, M. P., Lemaire, M., Georgopoulos, C. & Raina, S. (1997). Modulation of the Escherichia coli sE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol Microbiol 24, 355-371
    • (1997) Mol Microbiol , vol.24 , pp. 355-371
    • Missiakas, D.1    Mayer, M.P.2    Lemaire, M.3    Georgopoulos, C.4    Raina, S.5
  • 39
    • 14644440779 scopus 로고    scopus 로고
    • Transcriptome analysis of the Rhodobacter sphaeroides PpsR regulon: PpsR as a master regulator of photosystem development
    • Moskvin, O. V., Gomelsky, L. & Gomelsky, M. (2005). Transcriptome analysis of the Rhodobacter sphaeroides PpsR regulon: PpsR as a master regulator of photosystem development. J Bacteriol 187, 2148-2156
    • (2005) J Bacteriol , vol.187 , pp. 2148-2156
    • Moskvin, O.V.1    Gomelsky, L.2    Gomelsky, M.3
  • 40
    • 0033607497 scopus 로고    scopus 로고
    • The Rhodobacter sphaeroides ECF sigma factor, sE, and the target promoters cycA P3 and rpoE P1
    • Newman, J. D., Falkowski, M. J., Schilke, B. A., Anthony, L. C. & Donohue, T. J. (1999). The Rhodobacter sphaeroides ECF sigma factor, sE, and the target promoters cycA P3 and rpoE P1. J Mol Biol 294, 307-320
    • (1999) J Mol Biol , vol.294 , pp. 307-320
    • Newman, J.D.1    Falkowski, M.J.2    Schilke, B.A.3    Anthony, L.C.4    Donohue, T.J.5
  • 41
    • 58149503635 scopus 로고    scopus 로고
    • RpoHII activates oxidativestress defense systems and is controlled by RpoE in the singlet oxygendependent response in Rhodobacter sphaeroides
    • Nuss, A. M., Glaeser, J. & Klug, G. (2009). RpoHII activates oxidativestress defense systems and is controlled by RpoE in the singlet oxygendependent response in Rhodobacter sphaeroides. J Bacteriol 191, 220-230
    • (2009) J Bacteriol , vol.191 , pp. 220-230
    • Nuss, A.M.1    Glaeser, J.2    Klug, G.3
  • 44
    • 66849121542 scopus 로고    scopus 로고
    • Identification of the binding site of the s54 hetero-oligomeric FleQ/FleT activator in the flagellar promoters of Rhodobacter sphaeroides
    • Peña-Sánchez, J., Poggio, S., Flores-Pérez, U., Osorio, A., Domenzain, C., Dreyfus, G. & Camarena, L. (2009). Identification of the binding site of the s54 hetero-oligomeric FleQ/FleT activator in the flagellar promoters of Rhodobacter sphaeroides. Microbiology 155, 1669-1679
    • (2009) Microbiology , vol.155 , pp. 1669-1679
    • Peña-Sánchez, J.1    Poggio, S.2    Flores-Pérez, U.3    Osorio, A.4    Domenzain, C.5    Dreyfus, G.6    Camarena, L.7
  • 45
    • 79955977759 scopus 로고    scopus 로고
    • Response of the photosynthetic bacterium Rhodobacter sphaeroides to iron limitation and role of a Fur ortholog in this response
    • Peuser, V., Metz, S. & Klug, G. (2011). Response of the photosynthetic bacterium Rhodobacter sphaeroides to iron limitation and role of a Fur ortholog in this response. Environ Microbiol Rep 3, 397-404
    • (2011) Environ Microbiol Rep , vol.3 , pp. 397-404
    • Peuser, V.1    Metz, S.2    Klug, G.3
  • 46
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. (2001). A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29, e45.
    • (2001) Nucleic Acids Res , vol.e45 , pp. 29
    • Pfaffl, M.W.1
  • 47
    • 0029145921 scopus 로고
    • Co-ordinated regulation of amino sugar biosynthesis and degradation: The NagC repressor acts as both an activator and a repressor for the transcription of the glmUS operon and requires two separated NagC binding sites
    • Plumbridge, J. (1995). Co-ordinated regulation of amino sugar biosynthesis and degradation: the NagC repressor acts as both an activator and a repressor for the transcription of the glmUS operon and requires two separated NagC binding sites. EMBO J 14, 3958-3965
    • (1995) EMBO J , vol.14 , pp. 3958-3965
    • Plumbridge, J.1
  • 48
    • 0035863768 scopus 로고    scopus 로고
    • DNA binding sites for the Mlc and NagC proteins: Regulation of nagE, encoding the N-acetylglucosaminespecific transporter in Escherichia coli
    • Plumbridge, J. (2001). DNA binding sites for the Mlc and NagC proteins: regulation of nagE, encoding the N-acetylglucosaminespecific transporter in Escherichia coli. Nucleic Acids Res 29, 506-514
    • (2001) Nucleic Acids Res , vol.29 , pp. 506-514
    • Plumbridge, J.1
  • 49
    • 0029090774 scopus 로고
    • Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus
    • Pollich, M. & Klug, G. (1995). Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. J Bacteriol 177, 4481-4487
    • (1995) J Bacteriol , vol.177 , pp. 4481-4487
    • Pollich, M.1    Klug, G.2
  • 50
    • 0030467959 scopus 로고    scopus 로고
    • The bluF gene of Rhodobacter capsulatus is involved in conversion of cobinamide to cobalamin (vitamin B12)
    • Pollich, M., Wersig, C. & Klug, G. (1996). The bluF gene of Rhodobacter capsulatus is involved in conversion of cobinamide to cobalamin (vitamin B12). J Bacteriol 178, 7308-7310
    • (1996) J Bacteriol , vol.178 , pp. 7308-7310
    • Pollich, M.1    Wersig, C.2    Klug, G.3
  • 51
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P. & Krisch, H. M. (1984). In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29, 303-313
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 52
  • 54
    • 77955247454 scopus 로고    scopus 로고
    • An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signals
    • Purcell, E. B., McDonald, C. A., Palfey, B. A. & Crosson, S. (2010). An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signals. Biochemistry 49, 6761-6770
    • (2010) Biochemistry , vol.49 , pp. 6761-6770
    • Purcell, E.B.1    McDonald, C.A.2    Palfey, B.A.3    Crosson, S.4
  • 56
    • 0028934624 scopus 로고
    • ChrR positively regulates transcription of the Rhodobacter sphaeroides cytochrome c2 gene
    • Schilke, B. A. & Donohue, T. J. (1995). ChrR positively regulates transcription of the Rhodobacter sphaeroides cytochrome c2 gene. J Bacteriol 177, 1929-1937
    • (1995) J Bacteriol , vol.177 , pp. 1929-1937
    • Schilke, B.A.1    Donohue, T.J.2
  • 57
    • 0141848660 scopus 로고    scopus 로고
    • VIVID is a flavoprotein and serves as a fungal blue light photoreceptor for photoadaptation
    • Schwerdtfeger, C. & Linden, H. (2003). VIVID is a flavoprotein and serves as a fungal blue light photoreceptor for photoadaptation. EMBO J 22, 4846-4855
    • (2003) EMBO J , vol.22 , pp. 4846-4855
    • Schwerdtfeger, C.1    Linden, H.2
  • 58
    • 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
    • (1983) Nat Biotechnol , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 60
    • 0242333835 scopus 로고    scopus 로고
    • Normalization of cDNA microarray data
    • Smyth, G. K. & Speed, T. (2003). Normalization of cDNA microarray data. Methods 31, 265-273
    • (2003) Methods , vol.31 , pp. 265-273
    • Smyth, G.K.1    Speed, T.2
  • 61
    • 33749580770 scopus 로고    scopus 로고
    • The multitalented microbial sensory rhodopsins
    • Spudich, J. L. (2006). The multitalented microbial sensory rhodopsins. Trends Microbiol 14, 480-487
    • (2006) Trends Microbiol , vol.14 , pp. 480-487
    • Spudich, J.L.1
  • 63
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the secondmessenger c-di-GMP
    • Tarutina, M., Ryjenkov, D. A. & Gomelsky, M. (2006). An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the secondmessenger c-di-GMP. J BiolChem281, 34751-34758
    • (2006) J BiolChem , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 64
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L. & Zhulin, I. B. (1999). PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63, 479-506
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 65
    • 0034597011 scopus 로고    scopus 로고
    • Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold
    • van Aalten, D. M., DiRusso, C. C., Knudsen, J. & Wierenga, R. K. (2000). Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J 19, 5167-5177
    • (2000) EMBO J , vol.19 , pp. 5167-5177
    • van Aalten, D.M.1    Dirusso, C.C.2    Knudsen, J.3    Wierenga, R.K.4
  • 66
    • 0020698372 scopus 로고
    • Decay of mRNA in Escherichia coli: Investigation of the fate of specific segments of transcripts
    • von Gabain, A., Belasco, J. G., Schottel, J. L., Chang, A. C. & Cohen, S. N. (1983). Decay of mRNA in Escherichia coli: investigation of the fate of specific segments of transcripts. Proc Natl Acad Sci U S A 80, 653-657
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 653-657
    • von Gabain, A.1    Belasco, J.G.2    Schottel, J.L.3    Chang, A.C.4    Cohen, S.N.5
  • 67
    • 27144476747 scopus 로고    scopus 로고
    • Transcriptome and physiological responses to hydrogen peroxide of the facultatively phototrophic bacterium Rhodobacter sphaeroides
    • Zeller, T., Moskvin, O. V., Li, K., Klug, G. & Gomelsky, M. (2005). Transcriptome and physiological responses to hydrogen peroxide of the facultatively phototrophic bacterium Rhodobacter sphaeroides. J Bacteriol 187, 7232-7242
    • (2005) J Bacteriol , vol.187 , pp. 7232-7242
    • Zeller, T.1    Moskvin, O.V.2    Li, K.3    Klug, G.4    Gomelsky, M.5
  • 68
    • 46849107098 scopus 로고    scopus 로고
    • Light activation of the LOV protein Vivid generates a rapidly exchanging dimer
    • Zoltowski, B. D. & Crane, B. R. (2008). Light activation of the LOV protein Vivid generates a rapidly exchanging dimer. Biochemistry 47, 7012-7019.
    • (2008) Biochemistry , vol.47 , pp. 7012-7019
    • Zoltowski, B.D.1    Crane, B.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.