Using photoactivatable GFPs to study protein dynamics and function
Part 3. Proteomics
3.4. Functional Proteomics
Published Online: 15 APR 2005
Copyright © 2005 John Wiley & Sons, Ltd
Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics
How to Cite
Chudakov, D. M. and Lukyanov, K. A. 2005. Using photoactivatable GFPs to study protein dynamics and function. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.4:50.
- Published Online: 15 APR 2005
Green fluorescent protein (GFP) from jellyfish Aequorea victoria, its mutants, and homologs from other organisms have become an integral part of modern methodology in cell and molecular biology. GFP-like proteins represent the only genetically encoded fluorescent tags that can be widely used to label organisms, cells, organelles, and proteins. This review is focused on photoactivatable GFP-like proteins, that is, proteins capable of manyfold increase of fluorescence intensity at certain excitation-emission wavelengths in response to irradiation with specific light. Photoactivatable tags make it possible to “switch-on” fluorescent signal by a beam of light in precisely chosen part of organism or cell in order to track the movement of the labeled objects. The spectral properties and mechanisms of the photoactivation for the most experimentally useful photoconvertible proteins are described in detail. In particular, we discuss GFP and its mutant PA-GFP, green-to-red convertible protein Kaede from a stony coral Trachyphyllia geoffroyi, and kindling fluorescent protein (KFP) from a sea anemone Anemonia sulcata. Considerable progress is still required to enrich the palette of monomeric photoactivatable GFP-like proteins, which would extend the field of possible applications.
- fluorescent labeling;
- green fluorescent protein;