Structure and dynamics of green fluorescent protein.

Many marine organisms are luminescent. The proteins that produce the light include a primary light producer (aequorin or luciferase) and often a secondary photoprotein that red shifts the light for better penetration in the ocean. Green fluorescent protein is one such secondary protein. It is remarkable in that it autocatalyzes the formation of its own fluorophore and thus can be expressed in a variety of organisms in its fluorescent form. The recent determination of its 3D structure and other physical characterizations are revealing its molecular mechanism of action.

[1]  W. Stemmer,et al.  Improved Green Fluorescent Protein by Molecular Evolution Using DNA Shuffling , 1996, Nature Biotechnology.

[2]  Alexander Wlodawer,et al.  The structural basis for spectral variations in green fluorescent protein , 1997, Nature Structural Biology.

[3]  S. Boxer,et al.  Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[4]  B. Reid,et al.  Chromophore formation in green fluorescent protein. , 1997, Biochemistry.

[5]  S. Inouye,et al.  Chemical nature of the light emitter of the Aequorea green fluorescent protein. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

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

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

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

[9]  Tomoko Nakanishi,et al.  ‘Green mice’ as a source of ubiquitous green cells , 1997, FEBS letters.

[10]  G. Phillips,et al.  The molecular structure of green fluorescent protein , 1996, Nature Biotechnology.

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

[12]  J. L. Smith,et al.  Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[13]  R. Tsien,et al.  On/off blinking and switching behaviour of single molecules of green fluorescent protein , 1997, Nature.

[14]  Douglas C. Youvan,et al.  Time-resolved spectroscopy of wild-type and mutant Green Fluorescent Proteins reveals excited state deprotonation consistent with fluorophore-protein interactions , 1996 .

[15]  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.

[16]  A molecular mechanics and database analysis of the structural preorganization and activation of the chromophore-containing hexapeptide fragment in green fluorescent protein. , 1997, Journal of biomolecular structure & dynamics.

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

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

[19]  G. Schulz,et al.  Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution , 1994, Protein science : a publication of the Protein Society.

[20]  R. Mitra,et al.  Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. , 1996, Gene.

[21]  M. Oka,et al.  Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1. , 1995, Journal of biochemistry.

[22]  T. M. Horiagon,et al.  Deletion mapping of the Aequorea victoria green fluorescent protein. , 1996, Gene.

[23]  D. O'Kane,et al.  Green‐fluorescent protein mutants with altered fluorescence excitation spectra , 1995, FEBS letters.

[24]  S J Remington,et al.  Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[25]  P. Herring.  Bioluminescence in action , 1978 .

[26]  R. Tsien,et al.  Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer , 1996, Current Biology.

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

[28]  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.

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

[30]  M. D. Kemple,et al.  Proton nuclear magnetic resonance and fluorescence spectroscopic studies of segmental mobility in aequorin and a green fluorescent protein from aequorea forskalea. , 1980, Biophysical journal.

[31]  Roger Y. Tsien,et al.  Crystal Structure of the Aequorea victoria Green Fluorescent Protein , 1996, Science.

[32]  J. Haseloff,et al.  Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy. , 1995, Biochemical and biophysical research communications.

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