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A photoactivatable GFP for selective photolabeling of proteins and cells.

Science (New York, N.Y.) | Sep 13, 2002

We report a photoactivatable variant of the Aequorea victoria green fluorescent protein (GFP) that, after intense irradiation with 413-nanometer light, increases fluorescence 100 times when excited by 488-nanometer light and remains stable for days under aerobic conditions. These characteristics offer a new tool for exploring intracellular protein dynamics by tracking photoactivated molecules that are the only visible GFPs in the cell. Here, we use the photoactivatable GFP both as a free protein to measure protein diffusion across the nuclear envelope and as a chimera with a lysosomal membrane protein to demonstrate rapid interlysosomal membrane exchange.

Pubmed ID: 12228718 RIS Download

Mesh terms: Aerobiosis | Amino Acid Substitution | Antigens, CD | Cell Nucleus | Cytoplasm | Fluorescence | Green Fluorescent Proteins | Intracellular Membranes | Kinetics | Light | Luminescent Proteins | Lysosome-Associated Membrane Glycoproteins | Lysosomes | Membrane Glycoproteins | Nuclear Envelope | Protein Engineering | Protein Transport | Proteins | Recombinant Fusion Proteins | Spectrometry, Fluorescence

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