Abstract
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.
Keywords
Green fluorescent proteinAequorea victoriaChemistryFluorescenceBiophysicsChimera (genetics)Cell biologyMembrane proteinMembraneBiochemistryBiologyGenePhysics
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Publication Info
- Year
- 2002
- Type
- article
- Volume
- 297
- Issue
- 5588
- Pages
- 1873-1877
- Citations
- 1574
- Access
- Closed
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Cite This
George H. Patterson,
Jennifer Lippincott‐Schwartz
(2002).
A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells.
Science
, 297
(5588)
, 1873-1877.
https://doi.org/10.1126/science.1074952
Identifiers
- DOI
- 10.1126/science.1074952