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Publication Abstract from PubMed

Fluorescent protein (FP) variants that can be reversibly converted between fluorescent and nonfluorescent states have proven to be a catalyst for innovation in the field of fluorescence microscopy. However, the structural basis of the process remains poorly understood. High-resolution structures of a FP derived from Clavularia in both the fluorescent and the light-induced nonfluorescent states reveal that the rapid and complete loss of fluorescence observed upon illumination with 450-nm light results from cis-trans isomerization of the chromophore. The photoinduced change in configuration from the well ordered cis isomer to the highly nonplanar and disordered trans isomer is accompanied by a dramatic rearrangement of internal side chains. Taken together, the structures provide an explanation for the loss of fluorescence upon illumination, the slow light-independent recovery, and the rapid light-induced recovery of fluorescence. The fundamental mechanism appears to be common to all of the photoactivatable and reversibly photoswitchable FPs reported to date.

Structural basis for reversible photobleaching of a green fluorescent protein homologue.,Henderson JN, Ai HW, Campbell RE, Remington SJ Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6672-7. Epub 2007 Apr 9. PMID:17420458^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.