Green fluorescent protein

Photochem Photobiol. 1995 Oct;62(4):651-6. doi: 10.1111/j.1751-1097.1995.tb08712.x.

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 chromophore, 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.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cloning, Molecular
  • Cnidaria
  • Escherichia coli
  • Green Fluorescent Proteins
  • Luminescence
  • Luminescent Proteins / biosynthesis
  • Luminescent Proteins / chemistry*
  • Luminescent Proteins / metabolism
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Scyphozoa
  • Sequence Homology, Amino Acid

Substances

  • Luminescent Proteins
  • Recombinant Proteins
  • Green Fluorescent Proteins