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Volumn 368, Issue 5, 2007, Pages 1223-1230

The Critical Role of a Hydrogen Bond between Gln63 and Trp104 in the Blue-Light Sensing BLUF Domain That Controls AppA Activity

Author keywords

AppA; BLUF; flavin; photoreceptor; purple bacteria

Indexed keywords

GLUTAMINE; PROTEIN; PROTEIN APPA; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 34247263900     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.087     Document Type: Article
Times cited : (64)

References (45)
  • 1
    • 0036804709 scopus 로고    scopus 로고
    • BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms
    • Gomelsky M., and Klug G. BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms. Trends Biochem. Sci. 27 (2002) 497-500
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 497-500
    • Gomelsky, M.1    Klug, G.2
  • 2
    • 1642453927 scopus 로고    scopus 로고
    • Photoreceptor proteins, star actors of modern times: a review of the functional dynamics in the structure of representative members of six different photoreceptor families
    • van der Horst M.A., and Hellingwerf K.J. Photoreceptor proteins, star actors of modern times: a review of the functional dynamics in the structure of representative members of six different photoreceptor families. Accts. Chem. Res. 37 (2004) 13-20
    • (2004) Accts. Chem. Res. , vol.37 , pp. 13-20
    • van der Horst, M.A.1    Hellingwerf, K.J.2
  • 3
    • 84889314737 scopus 로고    scopus 로고
    • The antirepressor AppA uses the novel flavin-binding BLUF domain as blue-light-absorbing photoreceptor to control photosystem synthesis
    • Briggs W.R., and Spudich J. (Eds), Wiley-VCH Verlag GmbH, Weinheim
    • Masuda S., and Bauer C.E. The antirepressor AppA uses the novel flavin-binding BLUF domain as blue-light-absorbing photoreceptor to control photosystem synthesis. In: Briggs W.R., and Spudich J. (Eds). Handbook of Photosensory Receptors (2005), Wiley-VCH Verlag GmbH, Weinheim 433
    • (2005) Handbook of Photosensory Receptors , pp. 433
    • Masuda, S.1    Bauer, C.E.2
  • 4
    • 0001032488 scopus 로고
    • Blue-light irradiation reduces the expression of puf and puc operons of Rhodobacter sphaeroides under semi-aerobic conditions
    • Shimada H., Iba K., and Takamiya K. Blue-light irradiation reduces the expression of puf and puc operons of Rhodobacter sphaeroides under semi-aerobic conditions. Plant Cell Physiol. 33 (1992) 471-475
    • (1992) Plant Cell Physiol. , vol.33 , pp. 471-475
    • Shimada, H.1    Iba, K.2    Takamiya, K.3
  • 5
    • 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., and Kaplan S. 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 (1995) 4609-4618
    • (1995) J. Bacteriol. , vol.177 , pp. 4609-4618
    • Gomelsky, M.1    Kaplan, S.2
  • 6
    • 0031026315 scopus 로고    scopus 로고
    • Molecular genetic analysis suggesting interaction between AppA and PpsR in regulation of photosynthesis gene expression in R. sphaeroides 2.4.1
    • Gomelsky M., and Kaplan S. Molecular genetic analysis suggesting interaction between AppA and PpsR in regulation of photosynthesis gene expression in R. sphaeroides 2.4.1. J. Bacteriol. 179 (1997) 128-134
    • (1997) J. Bacteriol. , vol.179 , pp. 128-134
    • Gomelsky, M.1    Kaplan, S.2
  • 7
    • 0032567446 scopus 로고    scopus 로고
    • AppA, a redox regulator of photosystem formation in Rhodobacter sphaeroides 2.4.1, is a flavoprotein. Identification of a novel FAD binding domain
    • Gomelsky M., and Kaplan S. AppA, a redox regulator of photosystem formation in Rhodobacter sphaeroides 2.4.1, is a flavoprotein. Identification of a novel FAD binding domain. J. Biol. Chem. 273 (1998) 35319-35325
    • (1998) J. Biol. Chem. , vol.273 , pp. 35319-35325
    • Gomelsky, M.1    Kaplan, S.2
  • 8
    • 0036371637 scopus 로고    scopus 로고
    • A single flavoprotein, AppA, can integrate both redox and light signals in Rhodobacter sphaeroides
    • Braatsch S., Gomelsky M., Kuphal S., and Klug G. A single flavoprotein, AppA, can integrate both redox and light signals in Rhodobacter sphaeroides. Mol. Microbiol. 45 (2002) 827-836
    • (2002) Mol. Microbiol. , vol.45 , pp. 827-836
    • Braatsch, S.1    Gomelsky, M.2    Kuphal, S.3    Klug, G.4
  • 9
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • Masuda S., and Bauer C.E. AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. Cell 110 (2002) 613-623
    • (2002) Cell , vol.110 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 10
    • 4344656345 scopus 로고    scopus 로고
    • A eukaryotic BLUF domain mediates light-dependent gene expression in the purple bacterium Rhodobacter sphaeroides 2.4.1
    • Han Y., Braatsch S., Osterloh L., and Klug G. A eukaryotic BLUF domain mediates light-dependent gene expression in the purple bacterium Rhodobacter sphaeroides 2.4.1. Proc. Natl Acad. Sci. USA 101 (2004) 12306-12311
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12306-12311
    • Han, Y.1    Braatsch, S.2    Osterloh, L.3    Klug, G.4
  • 11
    • 33748961329 scopus 로고    scopus 로고
    • Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA
    • Kim S., Mason J.T., Knaff D.B., Bauer C.E., and Setterdahl A.T. Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA. Photosynth. Res. 89 (2006) 89-98
    • (2006) Photosynth. Res. , vol.89 , pp. 89-98
    • Kim, S.1    Mason, J.T.2    Knaff, D.B.3    Bauer, C.E.4    Setterdahl, A.T.5
  • 12
    • 13444291923 scopus 로고    scopus 로고
    • Light-induced structural changes of apoprotein and chromophore in the sensor of blue light using FAD (BLUF) domain of AppA for a signaling state
    • Masuda S., Hasegawa K., and Ono T. Light-induced structural changes of apoprotein and chromophore in the sensor of blue light using FAD (BLUF) domain of AppA for a signaling state. Biochemistry 44 (2005) 1215-1224
    • (2005) Biochemistry , vol.44 , pp. 1215-1224
    • Masuda, S.1    Hasegawa, K.2    Ono, T.3
  • 13
    • 0037984816 scopus 로고    scopus 로고
    • Spectroscopic and mutational analysis of the blue-light photoreceptor AppA: a novel photocycle involving flavin stacking with an aromatic amino acid
    • Kraft B.J., Masuda S., Kikuchi J., Dragnea V., Tollin G., Zaleski J.M., and Bauer C.E. Spectroscopic and mutational analysis of the blue-light photoreceptor AppA: a novel photocycle involving flavin stacking with an aromatic amino acid. Biochemistry 42 (2003) 6726-6734
    • (2003) Biochemistry , vol.42 , pp. 6726-6734
    • Kraft, B.J.1    Masuda, S.2    Kikuchi, J.3    Dragnea, V.4    Tollin, G.5    Zaleski, J.M.6    Bauer, C.E.7
  • 14
    • 0141844456 scopus 로고    scopus 로고
    • Initial characterization of the primary photochemistry of AppA, a blue-light-using flavin adenine dinucleotide-domain containing transcriptional antirepressor protein from Rhodobacter sphaeroides: a key role for reversible intramolecular proton transfer from the flavin adenine dinucleotide chromophore to a conserved tyrosine?
    • Laan W., van der Horst M.A., van Stokkum I.H., and Hellingwerf K.J. Initial characterization of the primary photochemistry of AppA, a blue-light-using flavin adenine dinucleotide-domain containing transcriptional antirepressor protein from Rhodobacter sphaeroides: a key role for reversible intramolecular proton transfer from the flavin adenine dinucleotide chromophore to a conserved tyrosine?. Photochem. Photobiol. 78 (2003) 290-297
    • (2003) Photochem. Photobiol. , vol.78 , pp. 290-297
    • Laan, W.1    van der Horst, M.A.2    van Stokkum, I.H.3    Hellingwerf, K.J.4
  • 15
    • 9744258714 scopus 로고    scopus 로고
    • Structural intermediate in the photocycle of a BLUF (sensor of blue light using FAD) protein Slr1694 in a cyanobacterium Synechocystis sp. PCC6803
    • Hasegawa K., Masuda S., and Ono T. Structural intermediate in the photocycle of a BLUF (sensor of blue light using FAD) protein Slr1694 in a cyanobacterium Synechocystis sp. PCC6803. Biochemistry 43 (2004) 14979-14986
    • (2004) Biochemistry , vol.43 , pp. 14979-14986
    • Hasegawa, K.1    Masuda, S.2    Ono, T.3
  • 16
    • 2442559284 scopus 로고    scopus 로고
    • Light-induced structural changes in a putative blue-light receptor with a novel FAD binding fold sensor of blue-light using FAD (BLUF); Slr1694 of Synechocystis sp. PCC6803
    • Masuda S., Hasegawa K., Ishii A., and Ono T. Light-induced structural changes in a putative blue-light receptor with a novel FAD binding fold sensor of blue-light using FAD (BLUF); Slr1694 of Synechocystis sp. PCC6803. Biochemistry 43 (2004) 5304-5313
    • (2004) Biochemistry , vol.43 , pp. 5304-5313
    • Masuda, S.1    Hasegawa, K.2    Ishii, A.3    Ono, T.4
  • 17
    • 20144368776 scopus 로고    scopus 로고
    • Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides
    • Anderson S., Dragnea V., Masuda S., Ybe J., Moffat K., and Bauer C. Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides. Biochemistry 44 (2005) 7998-8005
    • (2005) Biochemistry , vol.44 , pp. 7998-8005
    • Anderson, S.1    Dragnea, V.2    Masuda, S.3    Ybe, J.4    Moffat, K.5    Bauer, C.6
  • 18
    • 28944448536 scopus 로고    scopus 로고
    • Time-resolved spectroscopic studies of the AppA blue-light receptor BLUF domain from Rhodobacter sphaeroides
    • Dragnea V., Waegele M., Balascuta S., Bauer C., and Dragnea B. Time-resolved spectroscopic studies of the AppA blue-light receptor BLUF domain from Rhodobacter sphaeroides. Biochemistry 44 (2005) 15978-15985
    • (2005) Biochemistry , vol.44 , pp. 15978-15985
    • Dragnea, V.1    Waegele, M.2    Balascuta, S.3    Bauer, C.4    Dragnea, B.5
  • 19
    • 16344389152 scopus 로고    scopus 로고
    • Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, Tll0078, of Thermosynechococcus elongates BP-1
    • Fukushima Y., Okajima K., Shibata Y., Ikeuchi M., and Itoh S. Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, Tll0078, of Thermosynechococcus elongates BP-1. Biochemistry 44 (2005) 5149-5158
    • (2005) Biochemistry , vol.44 , pp. 5149-5158
    • Fukushima, Y.1    Okajima, K.2    Shibata, Y.3    Ikeuchi, M.4    Itoh, S.5
  • 20
    • 14844365385 scopus 로고    scopus 로고
    • Photocycle of the flavin-binding photoreceptor AppA, a bacterial transcriptional antirepressor of photosynthesis genes
    • Gauden M., Yeremenko S., Laan W., van Stokkum I.H.M., Ihalainen J.A., van Grondelle R., et al. Photocycle of the flavin-binding photoreceptor AppA, a bacterial transcriptional antirepressor of photosynthesis genes. Biochemistry 44 (2005) 3653-3662
    • (2005) Biochemistry , vol.44 , pp. 3653-3662
    • Gauden, M.1    Yeremenko, S.2    Laan, W.3    van Stokkum, I.H.M.4    Ihalainen, J.A.5    van Grondelle, R.6
  • 21
    • 14644435099 scopus 로고    scopus 로고
    • Spectroscopic analysis of the dark relaxation process of a photocycle in a sensor of blue light using FAD (BLUF) protein Slr1694 of the cyanobacterium Synechocystis sp. PCC6803
    • Hasegawa K., Masuda S., and Ono T. Spectroscopic analysis of the dark relaxation process of a photocycle in a sensor of blue light using FAD (BLUF) protein Slr1694 of the cyanobacterium Synechocystis sp. PCC6803. Plant Cell Physiol. 46 (2005) 136-146
    • (2005) Plant Cell Physiol. , vol.46 , pp. 136-146
    • Hasegawa, K.1    Masuda, S.2    Ono, T.3
  • 22
    • 25444486111 scopus 로고    scopus 로고
    • Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis
    • Ito S., Murakami A., Sato K., Nishina Y., Shiga K., Takahashi T., et al. Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis. Photochem. Photobiol. Sci. 4 (2005) 762-769
    • (2005) Photochem. Photobiol. Sci. , vol.4 , pp. 762-769
    • Ito, S.1    Murakami, A.2    Sato, K.3    Nishina, Y.4    Shiga, K.5    Takahashi, T.6
  • 23
    • 24644477536 scopus 로고    scopus 로고
    • Abstract structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction
    • Jung A., Domratcheva T., Tarutina M., Wu Q., Ko W.H., Shoeman R.L., et al. Abstract structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction. Proc. Natl Acad. Sci. USA 102 (2005) 12350-12355
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 12350-12355
    • Jung, A.1    Domratcheva, T.2    Tarutina, M.3    Wu, Q.4    Ko, W.H.5    Shoeman, R.L.6
  • 24
    • 18144372698 scopus 로고    scopus 로고
    • Structural of a cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue-light sensor domain
    • Kita A., Okajima K., Morimoto Y., Ikeuchi M., and Miki K. Structural of a cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue-light sensor domain. J. Mol. Biol. 349 (2005) 1-9
    • (2005) J. Mol. Biol. , vol.349 , pp. 1-9
    • Kita, A.1    Okajima, K.2    Morimoto, Y.3    Ikeuchi, M.4    Miki, K.5
  • 25
    • 23644434422 scopus 로고    scopus 로고
    • Adenosine diphosphate moitety does not participate in structural changes for the signaling state in the sensor of blue-light using FAD domain of AppA
    • Masuda S., Hasegawa K., and Ono T. Adenosine diphosphate moitety does not participate in structural changes for the signaling state in the sensor of blue-light using FAD domain of AppA. FEBS Letters 579 (2005) 4329-4332
    • (2005) FEBS Letters , vol.579 , pp. 4329-4332
    • Masuda, S.1    Hasegawa, K.2    Ono, T.3
  • 26
    • 30344475204 scopus 로고    scopus 로고
    • Tryptophan at position 104 is involved in transforming light signal into changes of β-sheet structure for the signaling state in the BLUF domain of AppA
    • Masuda S., Hasegawa K., and Ono T. Tryptophan at position 104 is involved in transforming light signal into changes of β-sheet structure for the signaling state in the BLUF domain of AppA. Plant Cell Physiol. 46 (2005) 1894-1901
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1894-1901
    • Masuda, S.1    Hasegawa, K.2    Ono, T.3
  • 27
    • 22744445702 scopus 로고    scopus 로고
    • Light-induced structural changes in the active site of the BLUF domain in AppA by Raman spectroscopy
    • Unno M., Sano R., Masuda S., Ono T., and Yamauchi S. Light-induced structural changes in the active site of the BLUF domain in AppA by Raman spectroscopy. J. Phys. Chem. B 109 (2005) 12620-12626
    • (2005) J. Phys. Chem. B , vol.109 , pp. 12620-12626
    • Unno, M.1    Sano, R.2    Masuda, S.3    Ono, T.4    Yamauchi, S.5
  • 28
    • 23044447414 scopus 로고    scopus 로고
    • Absorption and fluorescence spectroscopic characteriazation of BLUF domain of AppA from Rhodobacter sphaeroides
    • Zirak P., Penzkofer A., Schiereis T., Hegemann P., Jung A., and Schlichting I. Absorption and fluorescence spectroscopic characteriazation of BLUF domain of AppA from Rhodobacter sphaeroides. Chem. Phys. 315 (2005) 142-154
    • (2005) Chem. Phys. , vol.315 , pp. 142-154
    • Zirak, P.1    Penzkofer, A.2    Schiereis, T.3    Hegemann, P.4    Jung, A.5    Schlichting, I.6
  • 29
    • 34247258497 scopus 로고    scopus 로고
    • Two intermediate states I and J trapped at low temperature in the photocycles of two BLUF domain proteins of cyanobacteria Synechocystis sp. PCC6803 and Thermosynechococcus elongatus BP-1
    • Fukushima Y., Okajima K., Ikeuchi M., and Itoh S. Two intermediate states I and J trapped at low temperature in the photocycles of two BLUF domain proteins of cyanobacteria Synechocystis sp. PCC6803 and Thermosynechococcus elongatus BP-1. Photochem. Photobiol. 83 (2007) 112-121
    • (2007) Photochem. Photobiol. , vol.83 , pp. 112-121
    • Fukushima, Y.1    Okajima, K.2    Ikeuchi, M.3    Itoh, S.4
  • 31
    • 33845188381 scopus 로고    scopus 로고
    • Light-induced flipping of a conserved glutamine sidechain and its orientation in the AppA BLUF domain
    • Grinstead J.S., Avila-Perez M., Hellingwerf K.J., Boelens R., and Kaptein R. Light-induced flipping of a conserved glutamine sidechain and its orientation in the AppA BLUF domain. J. Am. Chem. Soc. 128 (2006) 15066-15067
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15066-15067
    • Grinstead, J.S.1    Avila-Perez, M.2    Hellingwerf, K.J.3    Boelens, R.4    Kaptein, R.5
  • 33
    • 33745728296 scopus 로고    scopus 로고
    • Tetramer formation kinetics in the signaling state of AppA monitored by time-resolved diffusion
    • Hazra P., Inoue K., Laan W., Hellingwerf K.J., and Terazima M. Tetramer formation kinetics in the signaling state of AppA monitored by time-resolved diffusion. Biophys. J. 91 (2006) 654-661
    • (2006) Biophys. J. , vol.91 , pp. 654-661
    • Hazra, P.1    Inoue, K.2    Laan, W.3    Hellingwerf, K.J.4    Terazima, M.5
  • 34
    • 33748300578 scopus 로고    scopus 로고
    • Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction
    • Jung A., Reinstein J., Domratcheva T., Shoeman R.L., and Schlichting I. Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction. J. Mol. Biol. 362 (2006) 717-732
    • (2006) J. Mol. Biol. , vol.362 , pp. 717-732
    • Jung, A.1    Reinstein, J.2    Domratcheva, T.3    Shoeman, R.L.4    Schlichting, I.5
  • 36
    • 33748770093 scopus 로고    scopus 로고
    • Fate determination of the flavin photoreceptions in the cyanobacterial blue light receptor TePixD (Tll0078)
    • Okajima K., Fukushima Y., Suzuki H., Kita A., Ochiai Y., Katayama M., et al. Fate determination of the flavin photoreceptions in the cyanobacterial blue light receptor TePixD (Tll0078). J. Mol. Biol. 363 (2006) 10-18
    • (2006) J. Mol. Biol. , vol.363 , pp. 10-18
    • Okajima, K.1    Fukushima, Y.2    Suzuki, H.3    Kita, A.4    Ochiai, Y.5    Katayama, M.6
  • 37
    • 33646549579 scopus 로고    scopus 로고
    • Orientation of a key glutamine residue in the BLUF domain from AppA revealed by mutagenesis, spectroscopy, and quantum chemical calculations
    • Unno M., Masuda S., Ono T., and Yamauchi S. Orientation of a key glutamine residue in the BLUF domain from AppA revealed by mutagenesis, spectroscopy, and quantum chemical calculations. J. Am. Chem. Soc. 128 (2006) 5638-5639
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5638-5639
    • Unno, M.1    Masuda, S.2    Ono, T.3    Yamauchi, S.4
  • 38
    • 33750317872 scopus 로고    scopus 로고
    • Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling
    • Yuan H., Anderson S., Masuda S., Dragnea V., Moffat K., and Bauer C.E. Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling. Biochemistry 45 (2006) 12687-12694
    • (2006) Biochemistry , vol.45 , pp. 12687-12694
    • Yuan, H.1    Anderson, S.2    Masuda, S.3    Dragnea, V.4    Moffat, K.5    Bauer, C.E.6
  • 39
    • 33751507013 scopus 로고    scopus 로고
    • Absorption and emission spectroscopic characterization of blue-light receptor Slr1694 from Synechocystis sp. PCC6803
    • Zirak P., Penzkofer A., Lehmpfuhl C., Mathes T., and Hegemann P. Absorption and emission spectroscopic characterization of blue-light receptor Slr1694 from Synechocystis sp. PCC6803. J. Photochem. Photobiol. B 86 (2007) 22-34
    • (2007) J. Photochem. Photobiol. B , vol.86 , pp. 22-34
    • Zirak, P.1    Penzkofer, A.2    Lehmpfuhl, C.3    Mathes, T.4    Hegemann, P.5
  • 40
    • 0039170162 scopus 로고
    • Action spectra for inhibition by light of accumulation of bacteriochlorophyll and carotenoid during aerobic growth of photosynthetic bacteria
    • Iba K., and Takamiya K. Action spectra for inhibition by light of accumulation of bacteriochlorophyll and carotenoid during aerobic growth of photosynthetic bacteria. Plant Cell Physiol. 30 (1989) 471-477
    • (1989) Plant Cell Physiol. , vol.30 , pp. 471-477
    • Iba, K.1    Takamiya, K.2
  • 41
    • 0021592032 scopus 로고
    • In vivo insertional mutagenesis with a selectable DNA fragment
    • Prentki P., and Krisch H.M. In vivo insertional mutagenesis with a selectable DNA fragment. Gene 29 (1984) 303-313
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 42
    • 0347622751 scopus 로고    scopus 로고
    • Null mutation of HvrA compensates for loss of an essential relA/spoT-like gene in Rhodobacter capsulatus
    • Masuda S., and Bauer C.E. Null mutation of HvrA compensates for loss of an essential relA/spoT-like gene in Rhodobacter capsulatus. J. Bacteriol. 186 (2004) 235-239
    • (2004) J. Bacteriol. , vol.186 , pp. 235-239
    • Masuda, S.1    Bauer, C.E.2
  • 43
    • 0021027842 scopus 로고
    • A broad host range mobilizing system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria
    • Simon R., Priefer U., and Puhler A. A broad host range mobilizing system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1 (1983) 784-791
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 44
    • 0026662710 scopus 로고
    • An improved suicide vector for construction of chromosomal insertion mutagenesis in bacteria
    • Penfold R., and Pemberton J.M. An improved suicide vector for construction of chromosomal insertion mutagenesis in bacteria. Gene 118 (1992) 145-146
    • (1992) Gene , vol.118 , pp. 145-146
    • Penfold, R.1    Pemberton, J.M.2
  • 45
    • 0030879863 scopus 로고    scopus 로고
    • Horizontal transfer of genes coding for the photosynthetic reaction centers of purple bacteria
    • Nagashima K.V.P., Hiraishi A., Shimada K., and Matsuura K. Horizontal transfer of genes coding for the photosynthetic reaction centers of purple bacteria. J. Mol. Evol. 45 (1997) 131-136
    • (1997) J. Mol. Evol. , vol.45 , pp. 131-136
    • Nagashima, K.V.P.1    Hiraishi, A.2    Shimada, K.3    Matsuura, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.