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Volumn 81, Issue 5, 2005, Pages 1145-1152

Mutational effects on protein structural changes and interdomain interactions in the blue-light sensing LOV protein YtvA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 27544498857     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2005-05-25-RA-541     Document Type: Article
Times cited : (33)

References (46)
  • 1
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • Losi, A., E. Polverini, B. Quest and W. Gärtner (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
  • 2
    • 0035208894 scopus 로고    scopus 로고
    • Phototropins: A new family of flavin-binding blue light receptors in plants
    • Briggs, W. R., J. M. Christie and M. Salomon (2001) Phototropins: A new family of flavin-binding blue light receptors in plants. Antioxid. Redox. Sign. 3, 775-788.
    • (2001) Antioxid. Redox. Sign. , vol.3 , pp. 775-788
    • Briggs, W.R.1    Christie, J.M.2    Salomon, M.3
  • 3
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential and light
    • Taylor, B. L. and I. B. Zhulin (1999) PAS domains: internal sensors of oxygen, redox potential and light. Microbiol. Mol. Biol. Res., 63, 479-506.
    • (1999) Microbiol. Mol. Biol. Res. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 4
    • 1642274684 scopus 로고    scopus 로고
    • The PAS fold: A redefinition of the PAS domain based upon structural prediction
    • Hefti, M. H., K. J. Francoijs, S. C. de Vries, R. Dixon and J. Vervoort (2004) The PAS fold: A redefinition of the PAS domain based upon structural prediction. FEBS J. 271, 1198-1208.
    • (2004) FEBS J. , vol.271 , pp. 1198-1208
    • Hefti, M.H.1    Francoijs, K.J.2    De Vries, S.C.3    Dixon, R.4    Vervoort, J.5
  • 5
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin mononucleotide
    • Christie, J. M., M. Salomon, K. Nozue, M. Wada and W. R. Briggs (1999) LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide. Proc. Natl. Acad. Sci. USA 96, 8779-8783.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8779-8783
    • Christie, J.M.1    Salomon, M.2    Nozue, K.3    Wada, M.4    Briggs, W.R.5
  • 7
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor phototropin
    • Salomon, M., J. M. Christie, E. Knieb, U. Lempert and W. R. Briggs (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor phototropin. Biochemistry 39, 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 9
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S. and K. Moffat (2002) Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 14, 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 10
    • 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., B. Quest and W. Gärtner (2003) Listening to the blue: the time-resolved thermodynamics of the bacterial blue-light receptor YtvA and its isolated LOV domain. Photochem. Photobiol. Sci. 2, 759-766.
    • (2003) Photochem. Photobiol. Sci. , vol.2 , pp. 759-766
    • Losi, A.1    Quest, B.2    Gärtner, W.3
  • 11
    • 3242747589 scopus 로고    scopus 로고
    • The bacterial counterparts of plants phototropins
    • Losi, A. (2004) The bacterial counterparts of plants phototropins. Photochem. Photobiol. Sci. 3, 566-574.
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 566-574
    • Losi, A.1
  • 12
    • 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., A. Losi, W. Gärtner, K.-E. Jaeger and T. Eggert (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
  • 13
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala, E., P. W. Oeller, E. Liscum, I. S. Han, E. Larsen and W. R. Briggs (1997) Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278, 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.S.4    Larsen, E.5    Briggs, W.R.6
  • 14
    • 0037446727 scopus 로고    scopus 로고
    • Mapping of low- and high-fluence autophosphorylation sites in phototropin 1
    • Salomon, M., E. Knieb, T. von Zeppelin and W. Rüdiger (2003) Mapping of low- and high-fluence autophosphorylation sites in phototropin 1. Biochemistry 42, 4217-4225.
    • (2003) Biochemistry , vol.42 , pp. 4217-4225
    • Salomon, M.1    Knieb, E.2    Von Zeppelin, T.3    Rüdiger, W.4
  • 15
    • 14744270377 scopus 로고    scopus 로고
    • Autophosphorylation, electrophoretic mobility and immunoreaction of oat phototropin 1 under UV and blue light paragraph sign
    • Knieb, E., M. Salomon and W. Rüdiger (2005) Autophosphorylation, electrophoretic mobility and immunoreaction of oat phototropin 1 under UV and blue light paragraph sign. Photochem. Photobiol. 81, 177-182.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 177-182
    • Knieb, E.1    Salomon, M.2    Rüdiger, W.3
  • 16
    • 0033953284 scopus 로고    scopus 로고
    • The STAS domain, a link between anion transporters and antisigma-factor antagonists
    • Aravind, L. and E. V. Koonin (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
  • 17
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie, J. M., T. E. Swartz, R. A. Bogomolni and W. R. Briggs (2002) Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J. 32, 205-219.
    • (2002) Plant J. , vol.32 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.A.3    Briggs, W.R.4
  • 18
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S. M., L. C. Neil and K. H. Gardner (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
  • 19
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jα helix interaction activates phototropin kinase activity
    • Harper, S. M., J. M. Christie and K. H. Gardner (2004) Disruption of the LOV-Jα 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
  • 20
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • Crosson, S., S. Rajagopal and K. Moffat (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
  • 21
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson, S. and K. Moffat (2001) Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc. Natl. Acad. Sci. USA 98, 2995-3000.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 22
    • 4644303602 scopus 로고    scopus 로고
    • Tryptophan Fluorescence in the Bacillus subtilis Phototropin-related Protein YtvA as a Marker of Interdomain Interaction
    • Losi, A., E. Ternelli and W. Gärtner (2004) Tryptophan Fluorescence in the Bacillus subtilis Phototropin-related Protein YtvA as a Marker of Interdomain Interaction. Photochem. Photobiol. 80, 150-153.
    • (2004) Photochem. Photobiol. , vol.80 , pp. 150-153
    • Losi, A.1    Ternelli, E.2    Gärtner, W.3
  • 23
    • 3242759944 scopus 로고    scopus 로고
    • Functional variations among LOV domains as revealed by FT-IR difference spectroscopy
    • Bednarz, T., A. Losi, W. Gärtner, P. Hegemann and J. Heberle (2004) Functional variations among LOV domains as revealed by FT-IR difference spectroscopy. Photochem. Photobiol. Sci. 3, 575-579.
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 575-579
    • Bednarz, T.1    Losi, A.2    Gärtner, W.3    Hegemann, P.4    Heberle, J.5
  • 24
    • 84945799762 scopus 로고
    • Fluorescence quantum yields of tryptophan and tyrosine
    • Chen, R. F. (1967) Fluorescence quantum yields of tryptophan and tyrosine. Anal. Lett. 1, 35-42.
    • (1967) Anal. Lett. , vol.1 , pp. 35-42
    • Chen, R.F.1
  • 26
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • Perczel, A., M. Hollosi, G. Tusnady and G. D. Fasman (1991) Convex constraint analysis: a natural deconvolution of circular dichroism curves of proteins. Protein Eng. 4, 669-679.
    • (1991) Protein Eng. , vol.4 , pp. 669-679
    • Perczel, A.1    Hollosi, M.2    Tusnady, G.3    Fasman, G.D.4
  • 27
    • 0026696116 scopus 로고
    • Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
    • Perczel, A., K. Park and G. D. Fasman (1992) Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide. Anal. Biochem. 203, 83-93.
    • (1992) Anal. Biochem. , vol.203 , pp. 83-93
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 30
    • 0035860102 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy of flavins and flavoenzymes: Photochemical and photophysical aspects
    • van den Berg, P. W., J. Widengren, M. A. Hink, R. Rigler and A. G. Visser (2001) Fluorescence correlation spectroscopy of flavins and flavoenzymes: photochemical and photophysical aspects. Spectrochim. Acta A 57, 2135-2144.
    • (2001) Spectrochim. Acta A , vol.57 , pp. 2135-2144
    • Van Den Berg, P.W.1    Widengren, J.2    Hink, M.A.3    Rigler, R.4    Visser, A.G.5
  • 31
    • 0010104094 scopus 로고    scopus 로고
    • PhotochemCAD: A computer-aided design and research tool in photochemistry
    • Du, H., R. A. Fuh, J. Li, A. Corkan and J. S. Lindsey (1998) PhotochemCAD: a computer-aided design and research tool in photochemistry. Photochem. Photobiol. 68, 141-142.
    • (1998) Photochem. Photobiol. , vol.68 , pp. 141-142
    • Du, H.1    Fuh, R.A.2    Li, J.3    Corkan, A.4    Lindsey, J.S.5
  • 33
    • 0018795179 scopus 로고
    • Electronic transitions in the isoalloxazine ring and orientation of flavins in model membranes studied by polarized light spectroscopy
    • Johansson, L. B., A. Davidsson, G. Lindblom and K. R. Naqvi (1979) Electronic transitions in the isoalloxazine ring and orientation of flavins in model membranes studied by polarized light spectroscopy. Biochemistry 18, 4249-4253.
    • (1979) Biochemistry , vol.18 , pp. 4249-4253
    • Johansson, L.B.1    Davidsson, A.2    Lindblom, G.3    Naqvi, K.R.4
  • 34
    • 0021096858 scopus 로고
    • Fluorescence depolarization of tryptophan residues in proteins: A molecular dynamics study
    • Ichiye, T. and M. Karplus (1983) Fluorescence depolarization of tryptophan residues in proteins: a molecular dynamics study. Biochemistry 22, 2884-2893.
    • (1983) Biochemistry , vol.22 , pp. 2884-2893
    • Ichiye, T.1    Karplus, M.2
  • 35
    • 0033035790 scopus 로고    scopus 로고
    • Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin
    • Tcherkasskaya, O. and O. B. Ptitsyn (1999) Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin. Protein Eng. 12, 485-490.
    • (1999) Protein Eng. , vol.12 , pp. 485-490
    • Tcherkasskaya, O.1    Ptitsyn, O.B.2
  • 36
  • 37
    • 0025194958 scopus 로고
    • Time-resolved fluorescence studies of flavodoxin. Fluorescence decay and fluorescence anisotropy decay of tryptophan in Desulfovibrio flavodoxins
    • Leenders, H. R., J. Vervoort, A. van Hoek and A. J. Visser (1990) Time-resolved fluorescence studies of flavodoxin. Fluorescence decay and fluorescence anisotropy decay of tryptophan in Desulfovibrio flavodoxins. Eur. Biophys. J. 18, 43-55.
    • (1990) Eur. Biophys. J. , vol.18 , pp. 43-55
    • Leenders, H.R.1    Vervoort, J.2    Van Hoek, A.3    Visser, A.J.4
  • 38
    • 0347499619 scopus 로고    scopus 로고
    • Correlating protein structure and protein fluorescence
    • Engelborghs, Y. (2003) Correlating protein structure and protein fluorescence. J. Fluoresc. 13, 9-16.
    • (2003) J. Fluoresc. , vol.13 , pp. 9-16
    • Engelborghs, Y.1
  • 39
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • Edited by R. A. Meyers John Wiley & Sons Ltd, Chichester, UK
    • Ladokhin, A. S. (2000) Fluorescence spectroscopy in peptide and protein analysis. In Encyclopedia of Analytical Chemistry (Edited by R. A. Meyers), pp. 5762-5779, John Wiley & Sons Ltd, Chichester, UK.
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762-5779
    • Ladokhin, A.S.1
  • 40
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • Fedorov, R., I. Schlichting, E. Hartmann, T. Domratcheva, M. Fuhrmann and P. Hegemann (2003) Crystal structures and molecular mechanism of a light-induced signaling switch: the Phot-LOV1 domain from Chlamydomonas reinhardtii. Biophys. J. 84, 2492-2501.
    • (2003) Biophys. J. , vol.84 , pp. 2492-2501
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 42
    • 0037428497 scopus 로고    scopus 로고
    • Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1
    • Corchnoy, S. B., T. E. Swartz, J. W. Lewis, I. Szundi, W. R. Briggs and R. A. Bogomolni (2003) Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1. J. Biol. Chem. 278, 724-731.
    • (2003) J. Biol. Chem. , vol.278 , pp. 724-731
    • Corchnoy, S.B.1    Swartz, T.E.2    Lewis, J.W.3    Szundi, I.4    Briggs, W.R.5    Bogomolni, R.A.6
  • 43
    • 0032574773 scopus 로고    scopus 로고
    • Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigma F of Bacillus subtilis
    • Kovacs, H., D. Comfort, M. Lord, I. D. Campbell and M. D. Yudkin (1998) Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigma F of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 95, 5067.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5067
    • Kovacs, H.1    Comfort, D.2    Lord, M.3    Campbell, I.D.4    Yudkin, M.D.5
  • 44
    • 2942616861 scopus 로고    scopus 로고
    • Photomorphogenesis in the hypogeous fungus Tuber borchii: Isolation and characterization of Tbwc-1, the homologue of the blue-light photoreceptor of Neurospora crassa
    • Ambra, R., B. Grimaldi, S. Zamboni, P. Filetici, G. Macino and P. Ballario (2004) Photomorphogenesis in the hypogeous fungus Tuber borchii: isolation and characterization of Tbwc-1, the homologue of the blue-light photoreceptor of Neurospora crassa. Fungal Genet. Biol. 41, 688-697.
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 688-697
    • Ambra, R.1    Grimaldi, B.2    Zamboni, S.3    Filetici, P.4    Macino, G.5    Ballario, P.6
  • 45
    • 16344374096 scopus 로고    scopus 로고
    • 2 sensing from structure-function relationships in the FixL proteins
    • 2 sensing from structure-function relationships in the FixL proteins. J. Inorg. Biochem. 99, 963-977.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 963-977
    • Rodgers, K.R.1    Lukat-Rodgers, G.S.2
  • 46
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling
    • Key, J. and K. Moffat (2005) Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 44, 4627-4635.
    • (2005) Biochemistry , vol.44 , pp. 4627-4635
    • Key, J.1    Moffat, K.2


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