Abstract

Green fluorescent proteins (GFPs) are presently attracting tremendous interest as the first general method to create strong visible fluorescence by purely molecular biological means. So far, they have been used as reporters of gene expression, tracers of cell lineage, and as fusion tags to monitor protein localization within living cells. However, the GFP originally cloned from the jellyfish Aequorea victoria has several nonoptimal properties including low brightness, a significant delay between protein synthesis and fluorescence development, and complex photoisomerization. Fortunately, the protein can be re-engineered by mutagenesis to ameliorate these deficiencies and shift the excitation and emission wavelengths, creating different colors and new applications.

Keywords

Aequorea victoriaGreen fluorescent proteinFluorescenceFluorescent proteinFusion proteinJellyfishProtein subcellular localization predictionMutagenesisProtein tagBiologyCell biologyBiophysicsGeneChemistryMutantBiochemistryPhysicsOptics

MeSH Terms

AnimalsCnidariaDictyosteliumGene ExpressionGreen Fluorescent ProteinsLuminescent MeasurementsLuminescent ProteinsMutagenesisProtein BindingProtein EngineeringSpectrometryFluorescence

Affiliated Institutions

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Publication Info

Year
1995
Type
review
Volume
20
Issue
11
Pages
448-455
Citations
1347
Access
Closed

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Cite This

A B Cubitt, Roger Heim, Stephen Adams et al. (1995). Understanding, improving and using green fluorescent proteins. Trends in Biochemical Sciences , 20 (11) , 448-455. https://doi.org/10.1016/s0968-0004(00)89099-4

Identifiers

DOI
10.1016/s0968-0004(00)89099-4
PMID
8578587

Data Quality

Data completeness: 81%