GREEN FLUORESCENT PROTEIN

Abstract— Several bioluminescent coelenterates use a secondary fluorescent protein, the green fluorescent protein (GFP), in an energy transfer reaction to produce green light. The most studied of these proteins have been the GFPs from the jellyfish Aequorea victoria and the sea pansy Renilla reniformis. Although the proteins from these organisms are not identical, they are thought to have the same chro‐mophore, which is derived from the primary amino acid sequence of GFP. The differences are thought to be due to changes in the protein environment of the chromophore. Recent interest in these molecules has arisen from the cloning of the Aequorea gfp cDNA and the demonstration that its expression in the absence of other Aequorea proteins results in a fluorescent product. This demonstration indicated that GFP could be used as a marker of gene expression and protein localization in living and fixed tissues. Bacterial, plant and animal (including mammalian) cells all express GFP. The heterologous expression of the gfp cDNA has also meant that it could be mutated to produce proteins with different fluorescent properties. Variants with more intense fluorescence or alterations in the excitation and emission spectra have been produced.

[1]  J. Nicol,et al.  Luminescence in Hydromedusae , 1955, Proceedings of the Royal Society of London. Series B - Biological Sciences.

[2]  J. Nicol Observations on luminescence in pelagic animals , 1958, Journal of the Marine Biological Association of the United Kingdom.

[3]  J. Nicol Observations on the luminescence of Pennatula phosphorea, with a note on the luminescence of Virgularia mirabilis , 1958, Journal of the Marine Biological Association of the United Kingdom.

[4]  J. R. Waters,et al.  Quantum efficiency of Cypridina luminescence, with a note on that of Aequorea† , 1962 .

[5]  O. Shimomura,et al.  Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. , 1962, Journal of cellular and comparative physiology.

[6]  J. W. Hastings,et al.  Energy transfer in a bioluminescent system , 1971, Journal of cellular physiology.

[7]  J. W. Hastings,et al.  Biochemistry of the bioluminescence of colonial hydroids and other coelenterates , 1971, Journal of cellular physiology.

[8]  M. J. Cormier,et al.  Structured bioluminescence. Two emitters during both the in vitro and the in vivo bioluminescence of the sea pansy, Renilla. , 1971, Biochemistry.

[9]  J. G. Morin X – Coelenterate Bioluminescence , 1974 .

[10]  O. Shimomura,et al.  Intermolecular energy transfer in the bioluminescent system of Aequorea. , 1974, Biochemistry.

[11]  M. J. Cormier,et al.  In vitro energy transfer in Renilla bioluminescence , 1976 .

[12]  William W. Ward,et al.  ENERGY TRANSFER VIA PROTEIN‐PROTEIN INTERACTION IN RENILLA BIOLUMINESCENCE , 1978 .

[13]  K. Mann,et al.  Chemical and physical properties of aequorin and the green fluorescent protein isolated from Aequorea forskålea. , 1978, Biochemistry.

[14]  W W Ward,et al.  An energy transfer protein in coelenterate bioluminescence. Characterization of the Renilla green-fluorescent protein. , 1979, The Journal of biological chemistry.

[15]  O. Shimomura,et al.  Structure of the chromophore of Aequorea green fluorescent protein , 1979 .

[16]  William W. Ward,et al.  Energy Transfer Processes in Bioluminescence , 1979 .

[17]  William W. Ward,et al.  SPECTROPHOTOMETRIC IDENTITY OF THE ENERGY TRANSFER CHROMOPHORES IN RENILLA AND AEQUOREA GREEN‐FLUORESCENT PROTEINS , 1980 .

[18]  W. Ward,et al.  Renaturation of Aequorea green-fluorescent protein , 1981 .

[19]  William W. Ward,et al.  SPECTRAL PERTURBATIONS OF THE AEQUOREA GREEN‐FLUORESCENT PROTEIN , 1982 .

[20]  W. Ward,et al.  Isolation and characterization of a photoprotein, “phialidin”, and a spectrally unique green-fluorescent protein from the bioluminescent jellyfish Phialidium gregarium , 1982 .

[21]  W. Ward,et al.  Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein. , 1982, Biochemistry.

[22]  Donald Boulter,et al.  Green Revolution , 1970 .

[23]  K. B. Ward,et al.  X-ray diffraction and time-resolved fluorescence analyses of Aequorea green fluorescent protein crystals. , 1988, The Journal of biological chemistry.

[24]  A. Fire,et al.  A modular set of lacZ fusion vectors for studying gene expression in Caenorhabditis elegans. , 1990, Gene.

[25]  M. J. Cormier,et al.  Primary structure of the Aequorea victoria green-fluorescent protein. , 1992, Gene.

[26]  C. Scharnagl,et al.  REVERSIBLE PHOTOCHEMISTRY IN THE α‐SUBUNIT OF PHYCOERYTHROCYANIN: CHARACTERIZATION OF CHROMOPHORE AND PROTEIN BY MOLECULAR DYNAMICS AND QUANTUM CHEMICAL CALCULATIONS , 1993 .

[27]  Kirkpatrick Sale,et al.  The green revolution , 1993 .

[28]  W. M. Westler,et al.  Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. , 1993, Biochemistry.

[29]  A. Murray,et al.  High resolution multimode digital imaging system for mitosis studies in vivo and in vitro. , 1994, The Biological bulletin.

[30]  Lawrence C. Katz,et al.  Neuronal transfection in brain slices using particle-mediated gene transfer , 1994, Neuron.

[31]  Martin Chalfie,et al.  Green fluorescent protein as a marker for gene expression , 1994 .

[32]  R Y Tsien,et al.  Wavelength mutations and posttranslational autoxidation of green fluorescent protein. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[33]  F. Tsuji,et al.  Aequorea green fluorescent protein , 1994, FEBS letters.

[34]  Cornelia I. Bargmann,et al.  The C. elegans gene odr-7 encodes an olfactory-specific member of the nuclear receptor superfamily , 1994, Cell.

[35]  T. Hazelrigg,et al.  Implications for bcd mRNA localization from spatial distribution of exu protein in Drosophila oogenesis , 1994, Nature.

[36]  S. Inouye,et al.  Evidence for redox forms of the Aequorea green fluorescent protein , 1994, FEBS letters.

[37]  M. Chalfie,et al.  Green fluorescent protein as a marker for gene expression. , 1994, Science.

[38]  Roger Y. Tsien,et al.  Improved green fluorescence , 1995, Nature.

[39]  D. Prasher,et al.  Using GFP to see the light. , 1995, Trends in genetics : TIG.

[40]  T. Hughes,et al.  The jellyfish green fluorescent protein: A new tool for studying ion channel expression and function , 1995, Neuron.

[41]  E. Fyrberg,et al.  Monitoring development and pathology of Drosophila indirect flight muscles using green fluorescent protein. , 1995, Developmental biology.

[42]  A. Coxon,et al.  Proteins that glow in green and blue. , 1995, Chemistry & biology.

[43]  T. Stearns,et al.  The green revolution , 1995 .

[44]  P. Silver,et al.  The GTP-bound form of the yeast Ran/TC4 homologue blocks nuclear protein import and appearance of poly(A)+ RNA in the cytoplasm. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[45]  Douglas C. Youvan,et al.  Red-Shifted Excitation Mutants of the Green Fluorescent Protein , 1995, Bio/Technology.

[46]  Tullio Pozzan,et al.  Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells , 1995, Current Biology.

[47]  R Y Tsien,et al.  Understanding, improving and using green fluorescent proteins. , 1995, Trends in biochemical sciences.