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Prof. Konstantin Lukyanov, Inst. of Bioorganic Chemistry, Moscow RUSSIA
Unusual fluorescent proteins: design and applications
The study and applications of fluorescent proteins has gone a long way from a subject of highly specialized research to a widely known and indispensable tool for in vivo labeling, and from a single known member¾Green Fluorescent Protein from Aequorea victoria¾to hundreds of natural proteins of different colors with still poorly studied phylogeny and biological significance [1].
My talk will be focused on fluorescent proteins with “unusual” spectral or biochemical characteristics. In particular, we developed KillerRed – phototoxic fluorescent protein capable of light-induced production of reactive oxygen species (ROS) [2]. KillerRed allows light-induced ROS production to be strictly localized to different compartments and subcompartments within a cell. It was shown that KillerRed-mediated oxidative stress at different locations results in clearly different molecular events and cell responses (e.g., triggering apoptosis for mitochondria-localized KillerRed, or DNA damage and temporal blockage of cell division for chromatin-localized KillerRed) [2, 3].
Recently, we designed CFP variant with an anionic tryptophan-based chromophore [4]. In contrast to green and red fluorescent proteins usually containing anionic tyrosine-based chromophores, no charged states of the CFP chromophore have been described before. We believe that switching between protonated and deprotonated tryptophan in chromophores of fluorescent proteins represents a new unexplored strategy to control their spectral properties.
For more information contact Dr. Kyril Solntsev (404-385-7131).