메뉴 건너뛰기




Volumn 7, Issue 1, 2012, Pages

Blue news update: BODIPY-GTP binds to the blue-light receptor YtvA while GTP does not

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BODIFY GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; UNCLASSIFIED DRUG; YTVA PROTEIN; 4,4 DIFLUORO 4 BORA 3A,4A DIAZA S INDACENE; 4,4-DIFLUORO-4-BORA-3A,4A-DIAZA-S-INDACENE; BORON DERIVATIVE; FLUORESCENT DYE; VISUAL PROTEINS AND PIGMENTS;

EID: 84855705834     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029201     Document Type: Article
Times cited : (7)

References (45)
  • 1
    • 77950377798 scopus 로고    scopus 로고
    • Light signal transduction: an infinite spectrum of possibilities
    • Chory J, (2010) Light signal transduction: an infinite spectrum of possibilities. Plant Journal 61: 982-991.
    • (2010) Plant Journal , vol.61 , pp. 982-991
    • Chory, J.1
  • 4
    • 72249087161 scopus 로고    scopus 로고
    • Distribution and Phylogeny of Light-Oxygen-Voltage-Blue-Light-Signaling Proteins in the Three Kingdoms of Life
    • Krauss U, Minh BQ, Losi A, Gartner W, Eggert T, et al. (2009) Distribution and Phylogeny of Light-Oxygen-Voltage-Blue-Light-Signaling Proteins in the Three Kingdoms of Life. Journal of Bacteriology 191: 7234-7242.
    • (2009) Journal of Bacteriology , vol.191 , pp. 7234-7242
    • Krauss, U.1    Minh, B.Q.2    Losi, A.3    Gartner, W.4    Eggert, T.5
  • 6
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper SM, Neil LC, Gardner KH, (2003) Structural basis of a phototropin light switch. Science 301: 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 7
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-J alpha helix interaction activates phototropin kinase activity
    • Harper SM, Christie JM, Gardner KH, (2004) Disruption of the LOV-J alpha helix interaction activates phototropin kinase activity. Biochemistry 43: 16184-16192.
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 8
    • 3242747589 scopus 로고    scopus 로고
    • The bacterial counterparts of plant phototropins
    • Losi A, (2004) The bacterial counterparts of plant phototropins. Photochemical & Photobiological Sciences 3: 566-574.
    • (2004) Photochemical & Photobiological Sciences , vol.3 , pp. 566-574
    • Losi, A.1
  • 9
    • 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
  • 10
    • 77957278505 scopus 로고    scopus 로고
    • The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study
    • Jurk M, Dorn M, Kikhney A, Svergun D, Gärtner W, et al. (2010) The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study. J Mol Biol 403: 78-87.
    • (2010) J Mol Biol , vol.403 , pp. 78-87
    • Jurk, M.1    Dorn, M.2    Kikhney, A.3    Svergun, D.4    Gärtner, W.5
  • 11
    • 0035141969 scopus 로고    scopus 로고
    • New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis
    • Akbar S, Gaidenko TA, Kang CM, O'Reilly M, Devine KM, et al. (2001) New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis. J Bacteriol 183: 1329-1338.
    • (2001) J Bacteriol , vol.183 , pp. 1329-1338
    • Akbar, S.1    Gaidenko, T.A.2    Kang, C.M.3    O'Reilly, M.4    Devine, K.M.5
  • 12
    • 33749021097 scopus 로고    scopus 로고
    • Blue light activates the sigmaB-dependent stress response of Bacillus subtilis via YtvA
    • Avila-Pérez M, Hellingwerf KJ, Kort R, (2006) Blue light activates the sigmaB-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
  • 13
    • 33749014144 scopus 로고    scopus 로고
    • The blue-light receptor YtvA acts in the environmental stress signaling pathway of Bacillus subtilis
    • Gaidenko TA, Kim TJ, Weigel AL, Brody MS, Price CW, (2006) The blue-light receptor YtvA acts in the environmental stress signaling pathway of Bacillus subtilis. J Bacteriol 188: 6387-6395.
    • (2006) J Bacteriol , vol.188 , pp. 6387-6395
    • Gaidenko, T.A.1    Kim, T.J.2    Weigel, A.L.3    Brody, M.S.4    Price, C.W.5
  • 14
    • 36049013726 scopus 로고    scopus 로고
    • Enhancement of a sigma(B)-dependent stress response in Bacillus subtilis by light via YtvA photoreceptor
    • Suzuki N, Takaya N, Hoshino T, Nakamura A, (2007) Enhancement of a sigma(B)-dependent stress response in Bacillus subtilis by light via YtvA photoreceptor. J Gen Appl Microbiol 53: 81-88.
    • (2007) J Gen Appl Microbiol , vol.53 , pp. 81-88
    • Suzuki, N.1    Takaya, N.2    Hoshino, T.3    Nakamura, A.4
  • 15
    • 1142304289 scopus 로고    scopus 로고
    • Listening to the blue: the time-resolved thermodynamics of the bacterial blue-light receptor YtvA and its isolated LOV domain
    • Losi A, Quest B, Gärtner W, (2003) Listening to the blue: the time-resolved thermodynamics of the bacterial blue-light receptor YtvA and its isolated LOV domain. Photochemical & Photobiological Sciences 2: 759-766.
    • (2003) Photochemical & Photobiological Sciences , vol.2 , pp. 759-766
    • Losi, A.1    Quest, B.2    Gärtner, W.3
  • 16
    • 38349092260 scopus 로고    scopus 로고
    • Molecular structure and regulation of phototropin kinase by blue light
    • Tokutomi S, Matsuoka D, Zikihara K, (2008) Molecular structure and regulation of phototropin kinase by blue light. Biochim Biophys Acta 1784: 133-142.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 133-142
    • Tokutomi, S.1    Matsuoka, D.2    Zikihara, K.3
  • 17
    • 46849107098 scopus 로고    scopus 로고
    • Light activation of the LOV protein vivid generates a rapidly exchanging dimer
    • Zoltowski BD, Crane BR, (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
  • 18
    • 70349777587 scopus 로고    scopus 로고
    • Structure and Signaling Mechanism of Per-ARNT-Sim Domains
    • Möglich A, Ayers RA, Moffat K, (2009) Structure and Signaling Mechanism of Per-ARNT-Sim Domains. Structure 17: 1282-1294.
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 19
    • 34548546911 scopus 로고    scopus 로고
    • Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA
    • Möglich A, Moffat K, (2007) Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA. J Mol Biol 373: 112-126.
    • (2007) J Mol Biol , vol.373 , pp. 112-126
    • Möglich, A.1    Moffat, K.2
  • 20
    • 58549105950 scopus 로고    scopus 로고
    • Design and signaling mechanism of light-regulated histidine kinases
    • Möglich A, Ayers RA, Moffat K, (2009) Design and signaling mechanism of light-regulated histidine kinases. J Mol Biol 385: 1433-1444.
    • (2009) J Mol Biol , vol.385 , pp. 1433-1444
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 21
    • 0033953284 scopus 로고    scopus 로고
    • The STAS domain - a link between anion transporters and antisigma-factor antagonists
    • Aravind L, Koonin EV, (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
  • 22
    • 0029904582 scopus 로고    scopus 로고
    • The SpoIIAA protein of Bacillus subtilis has GTP-binding properties
    • Najafi SMA, Harris DA, Yudkin MD, (1996) The SpoIIAA protein of Bacillus subtilis has GTP-binding properties. Journal of Bacteriology 178: 6632-6634.
    • (1996) Journal of Bacteriology , vol.178 , pp. 6632-6634
    • Najafi, S.M.A.1    Harris, D.A.2    Yudkin, M.D.3
  • 23
    • 79953159884 scopus 로고    scopus 로고
    • Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis
    • Sharma AK, Ye LW, Baer CE, Shanmugasundaram K, Alber T, et al. (2011) Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis. Journal of Biological Chemistry 286: 8534-8544.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 8534-8544
    • Sharma, A.K.1    Ye, L.W.2    Baer, C.E.3    Shanmugasundaram, K.4    Alber, T.5
  • 24
    • 0029958571 scopus 로고    scopus 로고
    • Protein motifs. 10. The GTP binding motif: Variations on a theme
    • Kjeldgaard M, Nyborg J, Clark BFC, (1996) Protein motifs. 10. The GTP binding motif: Variations on a theme. Faseb Journal 10: 1347-1368.
    • (1996) Faseb Journal , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 25
    • 33745404577 scopus 로고    scopus 로고
    • Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis
    • Buttani V, Losi A, Polverini E, Gärtner W, (2006) Blue news: NTP binding properties of the blue-light sensitive YtvA protein from Bacillus subtilis. FEBS Lett 580: 3818-3822.
    • (2006) FEBS Lett , vol.580 , pp. 3818-3822
    • Buttani, V.1    Losi, A.2    Polverini, E.3    Gärtner, W.4
  • 26
    • 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, et al. (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
  • 27
    • 34548591387 scopus 로고    scopus 로고
    • NTP-binding properties of the blue-light receptor YtvA and effects of the E105L mutation
    • Buttani V, Gärtner W, Losi A, (2007) NTP-binding properties of the blue-light receptor YtvA and effects of the E105L mutation. Eur Biophys J 36: 831-839.
    • (2007) Eur Biophys J , vol.36 , pp. 831-839
    • Buttani, V.1    Gärtner, W.2    Losi, A.3
  • 28
    • 74049123767 scopus 로고    scopus 로고
    • Interdomain signalling in the blue-light sensing and GTP-binding protein YtvA: A mutagenesis study uncovering the importance of specific protein sites
    • Tang YF, Cao Z, Livoti E, Krauss U, Jaeger KE, et al. (2010) Interdomain signalling in the blue-light sensing and GTP-binding protein YtvA: A mutagenesis study uncovering the importance of specific protein sites. Photochemical & Photobiological Sciences 9: 47-56.
    • (2010) Photochemical & Photobiological Sciences , vol.9 , pp. 47-56
    • Tang, Y.F.1    Cao, Z.2    Livoti, E.3    Krauss, U.4    Jaeger, K.E.5
  • 29
    • 79955414691 scopus 로고    scopus 로고
    • On the Binding of BODIPY-GTP by the Photosensory Protein YtvA from the Common Soil Bacterium Bacillus subtilis
    • Nakasone Y, Hellingwerf KJ, (2011) On the Binding of BODIPY-GTP by the Photosensory Protein YtvA from the Common Soil Bacterium Bacillus subtilis. Photochemistry and Photobiology 87: 542-547.
    • (2011) Photochemistry and Photobiology , vol.87 , pp. 542-547
    • Nakasone, Y.1    Hellingwerf, K.J.2
  • 30
    • 33845937672 scopus 로고    scopus 로고
    • Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: Application to adaptor protein complexes in cell signaling
    • Houtman JCD, Brown PH, Bowden B, Yamaguchi H, Appella E, et al. (2007) Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: Application to adaptor protein complexes in cell signaling. Protein Science 16: 30-42.
    • (2007) Protein Science , vol.16 , pp. 30-42
    • Houtman, J.C.D.1    Brown, P.H.2    Bowden, B.3    Yamaguchi, H.4    Appella, E.5
  • 31
    • 76649119460 scopus 로고    scopus 로고
    • Nonlinear least-squares data fitting in Excel spreadsheets
    • Kemmer G, Keller S, (2010) Nonlinear least-squares data fitting in Excel spreadsheets. Nature Protocols 5: 267-281.
    • (2010) Nature Protocols , vol.5 , pp. 267-281
    • Kemmer, G.1    Keller, S.2
  • 32
    • 80052769856 scopus 로고    scopus 로고
    • Revisiting the optimal c value for isothermal titration calorimetry
    • Broecker J, Vargas C, Keller S, (2011) Revisiting the optimal c value for isothermal titration calorimetry. Analytical Biochemistry 418: 307-309.
    • (2011) Analytical Biochemistry , vol.418 , pp. 307-309
    • Broecker, J.1    Vargas, C.2    Keller, S.3
  • 33
    • 80053033696 scopus 로고    scopus 로고
    • Blue Flickers of Hope: Secondary Structure, Dynamics and Putative Dimerisation Interface of the Blue-Light Receptor YtvA from Bacillus subtilis
    • Jurk M, Dorn M, Schmieder P, (2011) Blue Flickers of Hope: Secondary Structure, Dynamics and Putative Dimerisation Interface of the Blue-Light Receptor YtvA from Bacillus subtilis. Biochemistry 50 (38): 8163-8171.
    • (2011) Biochemistry , vol.50 , Issue.38 , pp. 8163-8171
    • Jurk, M.1    Dorn, M.2    Schmieder, P.3
  • 34
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M, Meyer B, (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. Journal of the American Chemical Society 123: 6108-6117.
    • (2001) Journal of the American Chemical Society , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 35
    • 0033789206 scopus 로고    scopus 로고
    • Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water
    • Dalvit C, Pevarello P, Tato M, Veronesi M, Vulpetti A, et al. (2000) Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water. Journal of biomolecular NMR 18: 65-68.
    • (2000) Journal of Biomolecular NMR , vol.18 , pp. 65-68
    • Dalvit, C.1    Pevarello, P.2    Tato, M.3    Veronesi, M.4    Vulpetti, A.5
  • 36
    • 0035692794 scopus 로고    scopus 로고
    • WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability
    • Dalvit C, Fogliatto G, Stewart A, Veronesi M, Stockman B, (2001) WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability. Journal of biomolecular NMR 21: 349-359.
    • (2001) Journal of Biomolecular NMR , vol.21 , pp. 349-359
    • Dalvit, C.1    Fogliatto, G.2    Stewart, A.3    Veronesi, M.4    Stockman, B.5
  • 37
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wuthrich K, (1997) Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proceedings of the National Academy of Sciences of the United States of America 94: 12366-12371.
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 39
    • 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
  • 40
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C, de Jong PJ, (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18: 6069-6074.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 41
    • 79954535201 scopus 로고
    • Molecular-Cloning - A Laboratory Manual, 2Nd Edition - Sambrook, J, Fritsch, Ef, Maniatis, T
    • Orkin S, (1990) Molecular-Cloning- A Laboratory Manual, 2Nd Edition- Sambrook, J, Fritsch, Ef, Maniatis, T. Nature 343: 604-605.
    • (1990) Nature , vol.343 , pp. 604-605
    • Orkin, S.1
  • 42
    • 34250682639 scopus 로고    scopus 로고
    • HCDF as a protein-labeling methodology - Production of H-2-, C-13-, and N-15-labeled OmpG via high cell density fermentation
    • Fiedler S, Knocke C, Vogt J, Oschkinat H, Diehl A, (2007) HCDF as a protein-labeling methodology- Production of H-2-, C-13-, and N-15-labeled OmpG via high cell density fermentation. Genetic Engineering & Biotechnology News 27: 54.
    • (2007) Genetic Engineering & Biotechnology News , vol.27 , pp. 54
    • Fiedler, S.1    Knocke, C.2    Vogt, J.3    Oschkinat, H.4    Diehl, A.5
  • 44
    • 7544243091 scopus 로고    scopus 로고
    • Uniform illumination of optically dense NMR samples
    • Kuprov I, Hore PJ, (2004) Uniform illumination of optically dense NMR samples. Journal of Magnetic Resonance 171: 171-175.
    • (2004) Journal of Magnetic Resonance , vol.171 , pp. 171-175
    • Kuprov, I.1    Hore, P.J.2
  • 45
    • 0026951903 scopus 로고
    • Gradient-Tailored Excitation for Single-Quantum Nmr-Spectroscopy of Aqueous-Solutions
    • Piotto M, Saudek V, Sklenar V, (1992) Gradient-Tailored Excitation for Single-Quantum Nmr-Spectroscopy of Aqueous-Solutions. Journal of biomolecular NMR 2: 661-665.
    • (1992) Journal of Biomolecular NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.