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Volumn 172, Issue 3, 2010, Pages 276-283

Fluorescence energy transfer in the bi-fluorescent S-layer tandem fusion protein ECFP-SgsE-YFP

Author keywords

Biocolloid; Fluorescence resonance energy transfer; Fluorescent proteins; S layer tandem fusion protein; Self assembly

Indexed keywords

BACTERIAL PROTEIN; ENHANCED CYAN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN; PROTEIN SGSE; SILICON DIOXIDE; UNCLASSIFIED DRUG; YELLOW ACCEPTOR PROTEIN;

EID: 77958189707     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.07.002     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 66149174918 scopus 로고    scopus 로고
    • Genetic engineering of the S-Layer protein SbpA of Lysinibacillus sphaericus CCM 2177 for the generation of functionalized nanoarrays
    • Badelt-Lichtblau H., Kainz B., Vollenkle C., Egelseer E.M., Sleytr U.B., Pum D., Ilk N. Genetic engineering of the S-Layer protein SbpA of Lysinibacillus sphaericus CCM 2177 for the generation of functionalized nanoarrays. Bioconjug. Chem. 2009, 20:895-903.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 895-903
    • Badelt-Lichtblau, H.1    Kainz, B.2    Vollenkle, C.3    Egelseer, E.M.4    Sleytr, U.B.5    Pum, D.6    Ilk, N.7
  • 2
    • 77958195806 scopus 로고    scopus 로고
    • in press. S-layers, nanobiotechnological applications. In: Flickinger, M.C. (Ed.), The Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Cell Technology. John Wiley & Sons, Inc., Hoboken, USA.
    • Egelseer, E.M., Ilk, N., Pum, D., Messner, P., Schäffer, C., Schuster, B., Sleytr, U.B., in press. S-layers, nanobiotechnological applications. In: Flickinger, M.C. (Ed.), The Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Cell Technology. John Wiley & Sons, Inc., Hoboken, USA.
    • Egelseer, E.M.1    Ilk, N.2    Pum, D.3    Messner, P.4    Schäffer, C.5    Schuster, B.6    Sleytr, U.B.7
  • 4
    • 15744403602 scopus 로고    scopus 로고
    • Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells
    • Galperin E., Verkhusha V.V., Sorkin A. Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells. Nat. Methods 2004, 1:209-217.
    • (2004) Nat. Methods , vol.1 , pp. 209-217
    • Galperin, E.1    Verkhusha, V.V.2    Sorkin, A.3
  • 6
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon G.W., Berry G., Liang X.H., Levine B., Herman B. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 1998, 74:2702-2713.
    • (1998) Biophys. J. , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 7
    • 10744224596 scopus 로고    scopus 로고
    • Flow cytometric measurement of fluorescence (Förster) resonance energy transfer from cyan fluorescent protein to yellow fluorescent protein using single-laser excitation at 458nm
    • He L., Bradrick T.D., Karpova T.S., Wu X., Fox M.H., Fischer R., McNally J.G., Knutson J.R., Grammer A.C., Lipsky P.E. Flow cytometric measurement of fluorescence (Förster) resonance energy transfer from cyan fluorescent protein to yellow fluorescent protein using single-laser excitation at 458nm. Cytometry A 2003, 53:39-54.
    • (2003) Cytometry A , vol.53 , pp. 39-54
    • He, L.1    Bradrick, T.D.2    Karpova, T.S.3    Wu, X.4    Fox, M.H.5    Fischer, R.6    McNally, J.G.7    Knutson, J.R.8    Grammer, A.C.9    Lipsky, P.E.10
  • 8
    • 39349116630 scopus 로고    scopus 로고
    • Structure prediction of an S-layer protein by the mean force method
    • Horejs C., Pum D., Sleytr U.B., Tscheliessnig R. Structure prediction of an S-layer protein by the mean force method. J. Chem. Phys. 2008, 128:065106.
    • (2008) J. Chem. Phys. , vol.128 , pp. 065106
    • Horejs, C.1    Pum, D.2    Sleytr, U.B.3    Tscheliessnig, R.4
  • 9
    • 75149112222 scopus 로고    scopus 로고
    • Designs and applications of fluorescent protein-based biosensors
    • Ibraheem A., Campbell R.E. Designs and applications of fluorescent protein-based biosensors. Curr. Opin. Chem. Biol. 2010, 14:30-36.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 30-36
    • Ibraheem, A.1    Campbell, R.E.2
  • 10
    • 2342576228 scopus 로고    scopus 로고
    • A functional chimaeric S-layer-enhanced green fluorescent protein to follow the uptake of S-layer-coated liposomes into eukaryotic cells
    • Ilk N., Küpcü S., Moncayo G., Klimt S., Ecker R.C., Hofer-Warbinek R., Egelseer E.M., Sleytr U.B., Sára M. A functional chimaeric S-layer-enhanced green fluorescent protein to follow the uptake of S-layer-coated liposomes into eukaryotic cells. Biochem. J. 2004, 379:441-448.
    • (2004) Biochem. J. , vol.379 , pp. 441-448
    • Ilk, N.1    Küpcü, S.2    Moncayo, G.3    Klimt, S.4    Ecker, R.C.5    Hofer-Warbinek, R.6    Egelseer, E.M.7    Sleytr, U.B.8    Sára, M.9
  • 11
    • 73949121127 scopus 로고    scopus 로고
    • Absorption, steady-state, fluorescence lifetime and 2D self-assembly properties of newly engineered fluorescence S-Layer fusion proteins of Geobacillus stearothermophilus NRS 2004/3a
    • Kainz B., Steiner K., Möller M., Pum D., Schäffer C., Sleytr U.B., Toca-Herrera J.L. Absorption, steady-state, fluorescence lifetime and 2D self-assembly properties of newly engineered fluorescence S-Layer fusion proteins of Geobacillus stearothermophilus NRS 2004/3a. Biomacromolecules 2010, 11:207-214.
    • (2010) Biomacromolecules , vol.11 , pp. 207-214
    • Kainz, B.1    Steiner, K.2    Möller, M.3    Pum, D.4    Schäffer, C.5    Sleytr, U.B.6    Toca-Herrera, J.L.7
  • 12
    • 73649103420 scopus 로고    scopus 로고
    • Identifying assembly-inhibiting and assembly-tolerant sites in the SbsB S-layer protein from Geobacillus stearothermophilus
    • Kinns H., Badelt-Lichtblau H., Egelseer E.M., Sleytr U.B., Howorka S. Identifying assembly-inhibiting and assembly-tolerant sites in the SbsB S-layer protein from Geobacillus stearothermophilus. J. Mol. Biol. 2010, 395:742-754.
    • (2010) J. Mol. Biol. , vol.395 , pp. 742-754
    • Kinns, H.1    Badelt-Lichtblau, H.2    Egelseer, E.M.3    Sleytr, U.B.4    Howorka, S.5
  • 16
    • 0022788452 scopus 로고
    • Characterization of the ultrastructure and the self-assembly of the surface layer of Bacillus stearothermophilus strain NRS 2004/3a
    • Messner P., Pum D., Sleytr U.B. Characterization of the ultrastructure and the self-assembly of the surface layer of Bacillus stearothermophilus strain NRS 2004/3a. J. Ultrastruct. Mol. Struct. Res. 1986, 97:73-88.
    • (1986) J. Ultrastruct. Mol. Struct. Res. , vol.97 , pp. 73-88
    • Messner, P.1    Pum, D.2    Sleytr, U.B.3
  • 17
  • 19
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen A.W., Daugherty P.S. Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 2005, 23:355-360.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 20
    • 67650568298 scopus 로고    scopus 로고
    • Engineering and exploiting protein assemblies in synthetic biology
    • Papapostolou D., Howorka S. Engineering and exploiting protein assemblies in synthetic biology. Mol. Biosyst. 2009, 5:723-732.
    • (2009) Mol. Biosyst. , vol.5 , pp. 723-732
    • Papapostolou, D.1    Howorka, S.2
  • 21
    • 10844242118 scopus 로고    scopus 로고
    • Molecular modeling of green fluorescent prote, structural effects of chromophore deprotonation
    • Patnaik S.S., Trohalaki S., Pachter R. Molecular modeling of green fluorescent prote, structural effects of chromophore deprotonation. Biopolymers 2004, 75:441-452.
    • (2004) Biopolymers , vol.75 , pp. 441-452
    • Patnaik, S.S.1    Trohalaki, S.2    Pachter, R.3
  • 22
    • 0034633010 scopus 로고    scopus 로고
    • Förster distances between green fluorescent protein pairs
    • Patterson G.H., Piston D.W., Barisas B.G. Förster distances between green fluorescent protein pairs. Anal. Biochem. 2000, 284:438-440.
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 23
    • 48149095082 scopus 로고    scopus 로고
    • The structure and binding behavior of the bacterial cell surface layer protein SbsC
    • Pavkov T., Egelseer E.M., Tesarz M., Svergun D.I., Sleytr U.B., Keller W. The structure and binding behavior of the bacterial cell surface layer protein SbsC. Structure 2008, 16:1226-1237.
    • (2008) Structure , vol.16 , pp. 1226-1237
    • Pavkov, T.1    Egelseer, E.M.2    Tesarz, M.3    Svergun, D.I.4    Sleytr, U.B.5    Keller, W.6
  • 24
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok B.A., Heim R. Using GFP in FRET-based applications. Trends Cell Biol. 1999, 9:57-60.
    • (1999) Trends Cell Biol. , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 27
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: scientific and practical applications
    • Sackmann E. Supported membranes: scientific and practical applications. Science 1996, 271:43-48.
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 28
    • 0028153924 scopus 로고
    • Isolation of two physiologically induced variant strains of Bacillus stearothermophilus NRS 2004/3a and characterization of their S-layer lattices
    • Sára M., Pum D., Küpcü S., Messner P., Sleytr U.B. Isolation of two physiologically induced variant strains of Bacillus stearothermophilus NRS 2004/3a and characterization of their S-layer lattices. J. Bacteriol. 1994, 176:848-860.
    • (1994) J. Bacteriol. , vol.176 , pp. 848-860
    • Sára, M.1    Pum, D.2    Küpcü, S.3    Messner, P.4    Sleytr, U.B.5
  • 29
    • 34548792373 scopus 로고    scopus 로고
    • Novel biocatalysts based on S-layer self-assembly of Geobacillus stearothermophilus NRS: a nanobiotechnological approach 2004/3a
    • Schäffer C., Novotny R., Küpcü S., Zayni S., Scheberl A., Friedmann J., Sleytr U.B., Messner P. Novel biocatalysts based on S-layer self-assembly of Geobacillus stearothermophilus NRS: a nanobiotechnological approach 2004/3a. Small 2007, 3:1549-1559.
    • (2007) Small , vol.3 , pp. 1549-1559
    • Schäffer, C.1    Novotny, R.2    Küpcü, S.3    Zayni, S.4    Scheberl, A.5    Friedmann, J.6    Sleytr, U.B.7    Messner, P.8
  • 31
    • 69249206640 scopus 로고    scopus 로고
    • Composite S-layer lipid structures
    • Schuster B., Sleytr U.B. Composite S-layer lipid structures. J. Struct. Biol. 2009, 168:207-216.
    • (2009) J. Struct. Biol. , vol.168 , pp. 207-216
    • Schuster, B.1    Sleytr, U.B.2
  • 32
    • 0030773829 scopus 로고    scopus 로고
    • Synthesis of cadmium sulphide superlattices using self-assembled bacterial S-layers
    • Shenton W., Pum D., Sleytr U.B., Mann S. Synthesis of cadmium sulphide superlattices using self-assembled bacterial S-layers. Nature 1997, 389:585-587.
    • (1997) Nature , vol.389 , pp. 585-587
    • Shenton, W.1    Pum, D.2    Sleytr, U.B.3    Mann, S.4
  • 34
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layer research: an overview
    • Sleytr U.B. Basic and applied S-layer research: an overview. FEMS Microbiol. Rev. 1997, 20:5-12.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 35
    • 0002587223 scopus 로고
    • The dynamic process of assembly of two-dimensional arrays of macromolecules on bacterial cell walls
    • Springer-Verlag, Berlin, Heidelberg, New York, W. Baumeister, W. Vogell (Eds.)
    • Sleytr U.B., Plohberger R. The dynamic process of assembly of two-dimensional arrays of macromolecules on bacterial cell walls. Electron Microscopy at Molecular Dimensions 1980, 36-47. Springer-Verlag, Berlin, Heidelberg, New York. W. Baumeister, W. Vogell (Eds.).
    • (1980) Electron Microscopy at Molecular Dimensions , pp. 36-47
    • Sleytr, U.B.1    Plohberger, R.2
  • 36
    • 0033583512 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S layers): from supramolecular cell structure to biomimetics and nanotechnology
    • Sleytr U.B., Messner P., Pum D., Sára M. Crystalline bacterial cell surface layers (S layers): from supramolecular cell structure to biomimetics and nanotechnology. Angew. Chem. Int. Ed. 1999, 38:1034-1054.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1034-1054
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sára, M.4
  • 37
    • 0002877469 scopus 로고    scopus 로고
    • Molecular nanotechnology and nanobiotechnology with two-dimensional protein crystals (S-layers)
    • Marcel Dekker, New York, M. Rosoff (Ed.)
    • Sleytr U.B., Pum D., Schuster B., Sára M. Molecular nanotechnology and nanobiotechnology with two-dimensional protein crystals (S-layers). Nano-Surface Chemistry 2001, 333-389. Marcel Dekker, New York. M. Rosoff (Ed.).
    • (2001) Nano-Surface Chemistry , pp. 333-389
    • Sleytr, U.B.1    Pum, D.2    Schuster, B.3    Sára, M.4
  • 39
    • 27944466452 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): a versatile self-assembly system. In: Ciferri, A. (Ed.), Supramolecular Polymers, CRC Press (Taylor & Francis Group), Boca Raton, Florida, 2005,
    • Sleytr, U.B., Sára, M., Pum, D., Schuster, B., 2005. Crystalline bacterial cell surface layers (S-layers): a versatile self-assembly system. In: Ciferri, A. (Ed.), Supramolecular Polymers, CRC Press (Taylor & Francis Group), Boca Raton, Florida, 2005, pp. 583-612.
    • (2005) , pp. 583-612
    • Sleytr, U.B.1    Sára, M.2    Pum, D.3    Schuster, B.4
  • 40
    • 33846006521 scopus 로고    scopus 로고
    • S-layers as a basic building block in a molecular construction kit
    • Sleytr U.B., Egelseer E.M., Ilk N., Pum D., Schuster B. S-layers as a basic building block in a molecular construction kit. FEBS J. 2007, 274:323-334.
    • (2007) FEBS J. , vol.274 , pp. 323-334
    • Sleytr, U.B.1    Egelseer, E.M.2    Ilk, N.3    Pum, D.4    Schuster, B.5
  • 41
    • 37349026887 scopus 로고    scopus 로고
    • Exploitation of the S-layer self-assembly system for site directed immobilization of enzymes demonstrated for an extremophilic laminarinase from Pyrococcus furiosus
    • Tschiggerl H., Breitwieser A., de Roo G., Verwoerd T., Schäffer C., Sleytr U.B. Exploitation of the S-layer self-assembly system for site directed immobilization of enzymes demonstrated for an extremophilic laminarinase from Pyrococcus furiosus. J. Biotechnol. 2008, 133:403-411.
    • (2008) J. Biotechnol. , vol.133 , pp. 403-411
    • Tschiggerl, H.1    Breitwieser, A.2    de Roo, G.3    Verwoerd, T.4    Schäffer, C.5    Sleytr, U.B.6
  • 42
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 1998, 67:509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 43
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe H., Periasamy A. Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 2005, 16:19-27.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2


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