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Volumn 105, Issue 33, 2008, Pages 11715-11719

PixE promotes dark oligomerization of the BLUF photoreceptor PixD

Author keywords

Flavin chromophore; Phototaxis; Synechocystis

Indexed keywords

BACTERIAL PROTEIN; PROTEIN PIXD; PROTEIN PIXE; QUERCETIN;

EID: 50149099155     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0802149105     Document Type: Article
Times cited : (59)

References (26)
  • 1
    • 84889314737 scopus 로고    scopus 로고
    • The antirepressor AppA uses the novel flavin-binding BLUF domain as a blue-light-absorbing photoreceptor to control photosystem synthesis
    • eds Briggs WR, Spudich JL Wiley, New York, pp
    • Masuda S, Bauer CE (2004) The antirepressor AppA uses the novel flavin-binding BLUF domain as a blue-light-absorbing photoreceptor to control photosystem synthesis. Handbook of Photosensory Receptors, eds Briggs WR, Spudich JL (Wiley, New York), pp 433-445.
    • (2004) Handbook of Photosensory Receptors , pp. 433-445
    • Masuda, S.1    Bauer, C.E.2
  • 2
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in. Rhodobacter sphaeroides
    • Masuda S, Bauer CE (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
  • 3
    • 0029093864 scopus 로고
    • appA, a novel gene encoding a trans-acting factor involved in the regulation of photosynthesis gene expression in Rhodobacter sphaeroides
    • 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. J Bacteriol 177:4609-4618.
    • (1995) J Bacteriol , vol.177 , pp. 4609-4618
    • Gomelsky, M.1    Kaplan, S.2
  • 4
    • 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, Kaplan S (1998) 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 273:35319-35325.
    • (1998) J Biol Chem , vol.273 , pp. 35319-35325
    • Gomelsky, M.1    Kaplan, S.2
  • 5
    • 33746653375 scopus 로고    scopus 로고
    • Hydrogen-bond switching through a radical pair mechanism in a flavin-binding photoreceptor
    • Gauden M, et al. (2006) Hydrogen-bond switching through a radical pair mechanism in a flavin-binding photoreceptor. Proc Natl Acad Sci USA 103:10895-10900.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10895-10900
    • Gauden, M.1
  • 6
    • 28944448536 scopus 로고    scopus 로고
    • Time-resolved spectroscopic studies of the AppA blue-light receptor BLUF domain from Rhodobacter sphaeroides
    • Dragnea V, et al. (2005) Time-resolved spectroscopic studies of the AppA blue-light receptor BLUF domain from Rhodobacter sphaeroides. Biochemistry 44:15978-15985.
    • (2005) Biochemistry , vol.44 , pp. 15978-15985
    • Dragnea, V.1
  • 7
    • 33748300578 scopus 로고    scopus 로고
    • Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction
    • Jung A, et al. (2006) Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction. J Mol Biol 362:717-732.
    • (2006) J Mol Biol , vol.362 , pp. 717-732
    • Jung, A.1
  • 8
    • 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 TA, Yamauchi S (2006) Orientation of a key glutamine residue in the BLUF domain from AppA revealed by mutagenesis, spectroscopy, and quantum chemical calculations. J Am Chem Soc 128:5638-5639.
    • (2006) J Am Chem Soc , vol.128 , pp. 5638-5639
    • Unno, M.1    Masuda, S.2    Ono, T.A.3    Yamauchi, S.4
  • 9
    • 33845188381 scopus 로고    scopus 로고
    • Light-induced flipping of a conserved glutamine side chain and its orientation in the AppA BLUF domain
    • Grinstead JS, et al. (2006) Light-induced flipping of a conserved glutamine side chain and its orientation in the AppA BLUF domain. J Am Chem Soc 128:15066-15067.
    • (2006) J Am Chem Soc , vol.128 , pp. 15066-15067
    • Grinstead, J.S.1
  • 10
    • 33750317872 scopus 로고    scopus 로고
    • Crystal structures of the synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling
    • Yuan H, et al. (2006) Crystal structures of the synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling. Biochemistry 45:12687-12694.
    • (2006) Biochemistry , vol.45 , pp. 12687-12694
    • Yuan, H.1
  • 11
    • 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, Ono TA (2004) 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 43:5304-5313.
    • (2004) Biochemistry , vol.43 , pp. 5304-5313
    • Masuda, S.1    Hasegawa, K.2    Ishii, A.3    Ono, T.A.4
  • 12
    • 34247263900 scopus 로고    scopus 로고
    • The critical role of a hydrogen bond between Gln63 and Trp104 in the blue-light sensing BLUF domain that controls AppA activity
    • Masuda S, Tomida Y, Ohta H, Takamiya K (2007) The critical role of a hydrogen bond between Gln63 and Trp104 in the blue-light sensing BLUF domain that controls AppA activity. J Mol Biol 368:1223-1230.
    • (2007) J Mol Biol , vol.368 , pp. 1223-1230
    • Masuda, S.1    Tomida, Y.2    Ohta, H.3    Takamiya, K.4
  • 13
    • 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, Ono TA (2005) 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 44:1215-1224.
    • (2005) Biochemistry , vol.44 , pp. 1215-1224
    • Masuda, S.1    Hasegawa, K.2    Ono, T.A.3
  • 14
    • 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, Ono TA (2005) 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 46:1894-1901.
    • (2005) Plant Cell Physiol , vol.46 , pp. 1894-1901
    • Masuda, S.1    Hasegawa, K.2    Ono, T.A.3
  • 15
    • 34250890102 scopus 로고    scopus 로고
    • On the role of aromatic side chains in the photoactivation of BLUF domains
    • Gauden M, et al. (2007) On the role of aromatic side chains in the photoactivation of BLUF domains. Biochemistry 46:7405-7415.
    • (2007) Biochemistry , vol.46 , pp. 7405-7415
    • Gauden, M.1
  • 16
    • 0037186598 scopus 로고    scopus 로고
    • A blue-light-activated adenylyl cyclase mediates photoavoidance in Euglena gracilis
    • Iseki M, et al. (2002) A blue-light-activated adenylyl cyclase mediates photoavoidance in Euglena gracilis. Nature 415:1047-1051.
    • (2002) Nature , vol.415 , pp. 1047-1051
    • Iseki, M.1
  • 17
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T, et al. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res 3:109-136.
    • (1996) DNA Res , vol.3 , pp. 109-136
    • Kaneko, T.1
  • 18
    • 7544245885 scopus 로고    scopus 로고
    • Biochemical characterization of the major adenylyl cyclase, Cya1, in the cyanobacterium Synechocystis sp PCC 6803
    • Masuda S, Ono TA (2004) Biochemical characterization of the major adenylyl cyclase, Cya1, in the cyanobacterium Synechocystis sp PCC 6803. FEBS Lett 577:255-258.
    • (2004) FEBS Lett , vol.577 , pp. 255-258
    • Masuda, S.1    Ono, T.A.2
  • 19
    • 2442454713 scopus 로고    scopus 로고
    • Structural and functional analysis of a novel flavoprotein in cyanobacteria
    • Okajima K, et al. (2003) Structural and functional analysis of a novel flavoprotein in cyanobacteria. Plant Cell Physiol 44:S162.
    • (2003) Plant Cell Physiol , vol.44
    • Okajima, K.1
  • 20
    • 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
  • 21
    • 22344445758 scopus 로고    scopus 로고
    • Biochemical and functional characterization of BLUF-type flavin-binding proteins of two species of cyanobacteria
    • Okajima K, et al. (2005) Biochemical and functional characterization of BLUF-type flavin-binding proteins of two species of cyanobacteria. J Biochem (Tokyo) 137:741-750.
    • (2005) J Biochem (Tokyo) , vol.137 , pp. 741-750
    • Okajima, K.1
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372:774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 24644477536 scopus 로고    scopus 로고
    • Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction
    • Jung A, et al. (2005) Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction. Proc Natl Acad Sci USA 102:12350-12355.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12350-12355
    • Jung, A.1
  • 24
    • 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 BJ, et al. (2003) Spectroscopic and mutational analysis of the blue-light photoreceptor AppA: A novel photocycle involving flavin stacking with an aromatic amino acid. Biochemistry 42:6726-6734.
    • (2003) Biochemistry , vol.42 , pp. 6726-6734
    • Kraft, B.J.1
  • 25
    • 33744816438 scopus 로고    scopus 로고
    • ltraScan: A comprehensive data analysis software package for analytical ultracentrifugation experiments
    • eds Scott DJ, Harding SE, Rowe AJ Royal Society of Chemistry, London, pp
    • Demeler B (2005) ltraScan: A comprehensive data analysis software package for analytical ultracentrifugation experiments. Modern Analytical Ultracentrifugation: Techniques and Methods, eds Scott DJ, Harding SE, Rowe AJ (Royal Society of Chemistry, London), pp 210-229.
    • (2005) Modern Analytical Ultracentrifugation: Techniques and Methods , pp. 210-229
    • Demeler, B.1
  • 26
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • ed Hinz H-J Springer, New York, pp
    • Durchschlag H (1986) Specific volumes of biological macromolecules and some other molecules of biological interest. Thermodynamic Data for Biochemistry and Biotechnology, ed Hinz H-J (Springer, New York), pp 45-128.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durchschlag, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.