Contact Us | Carl Zeiss

Zeiss Logo

Education in Microscopy and Digital Imaging

ZEISS Home ¦ Products ¦ Solutions ¦ Support ¦ Online Shop ¦ ZEISS International

Microscopy Reference Library

Aequorea victoria Fluorescent Proteins

Explore the early research reports involved with elucidating the structure and function of luminescent and fluorescent proteins derived from the Pacific jellyfish, Aequorea victoria. Papers by Osamu Shimomura, Martin Chalfie, and Roger Tsien described research that eventually resulted in the 2008 Nobel Prize in Chemistry being awarded to these investigators. Other reports listed in this section describe elucidation of the chromophore structure, the first cloning of cDNA for GFP, and the discovery of excited state proton transfer in fluorescent proteins.

Davenport, D. and Nicol, J. A. C.

Luminescence in Hydromedusae.  Proceedings of the Royal Society of London Series B-Biological Sciences 144: 399-411 (1955).  One of the first investigations to report on the luminescent responses of jellyfish, including species from Aequorea, Halistaura, Phialidium, and Stomotoca. The authors report luminous points corresponding to yellow-green fluorescent masses in the marginal canal of Aequorea jellyfish.

Shimomura, O., Johnson, F. H., and Saiga, Y.

Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea.  Journal of Cellular and Comparative Physiology 59: 223-239 (1962).  The original report on the isolation of aequorin from the Aequorea victoria jellyfish along with a brief discussion of the properties. The authors note the response of aequorin to calcium cations being the emission of a "flash of light" in aqueous medium.

Shimomura, O. and Johnson, F. H.

Properties of the bioluminescent protein aequorin.  Biochemistry 8: 3991-3997 (1969).  Characterization of the protein aequorin and separation of the protein into components that exhibit two distinct spectral profiles. The green fluorescent component is referred to as AF-400 and is removed from aequorin by treatment with sodium bisulfate.

Morin, J. G. and Hastings, J. W.

Biochemistry of Bioluminescence of Colonial Hydroids and Other Coelenterates.  Journal of Cellular Physiology 77: 313-318 (1971).  The authors describe calcium-mediated energy transfer from aequorin to the green fluorescent protein with emission at 508 nanometers, and suggest the latter could be a useful tool for investigations using fluorescence microscopy.

Prasher, D., McCann, R. O., and Cormier, M. J.

Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein.  Biochemical and Biophysical Research Communications 126: 1259-1268 (1985).  The first report on cloning aequorin cDNA using what is now considered to be antique technology. Dr. Prasher and colleagues were able to identify cloned apoaequorin from an extract recovered in E. coli expressing pBR322 plasmid vectors.

Prasher, D. C., Eckenrode, V. K., Ward, W. W., Prendergast, F. G., and Cormier, M. J.

Primary structure of the Aequorea victoria green-fluorescent protein.  Gene 111: 229-233 (1992).  Original report on the characterization of GFP from Aequorea victoria (referred to as gfp10), which encodes a 238-amino acid polypeptide with a calculated molecular weight of 26,888. The authors suggest that the gfp gene is comprised of at least three exons spread over 2,600 basepairs.

Cody, C. W., Prasher, D. C., Westler, W. M., Prendergast, F. G., and Ward, W. W.

Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein.  Biochemistry 32: 1212-1218 (1993).  Douglas Prasher and colleagues describe the characterization of the Aequorea victoria GFP chromophore (Ser-Tyr-Gly), which is released as a hexapeptide upon digestion of the protein with papain.

Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W., and Prasher, D. C.

Green fluorescent protein as a marker for gene expression.  Science 263: 802-805 (1994).  An elegant demonstration of GFP expression in bacteria (E. coli) and eukaryotic (C. elegans) cells that wound up on the cover of the journal and ultimately won the Nobel prize for Dr. Martin Chalfie. In worms, GFP was expressed under the control of a promoter that controls the gene for beta-tubulin.

Heim, R., Prasher, D. C., and Tsien, R. Y.

Wavelength mutations and posttranslational autoxidation of green fluorescent protein.  Proceedings of the National Academy of Sciences of the United States of America 91: 12501-12504 (1994).  Douglas Prasher teamed up with Roger Tsien's group to create GFP variants having aromatic and heterocyclic amino acids at position 66. Substitution of histidine for tyrosine resulted in blue fluorescence, whereas substitution of tryptophan produced cyan fluorescence.

Brejc, K., Sixma, T., Kitts, P. A., Kain, S. R., Tsien, R. Y., Ormo, M., and Remington, S. J.

Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein.  Proceedings of the National Academy of Sciences of the United States of America 94: 2306-2311 (1997).  Examination of the bimodal absorption spectrum of GFP coupled with an explanation of why excitation at 395 nanometers gives rise to fluorescence at 508 nanometers. The authors propose excited state proton transfer from the tyrosine at position 66 to glutamic acid at position 222.