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an enhanced monomeric blue fluorescent protein with the high chemical stability of the chromophore一个增强的单体的蓝色荧光蛋白发色团的化学稳定性高
An Enhanced Monomeric Blue Fluorescent Protein with
the High Chemical Stability of the Chromophore
1 2 2 1
Oksana M. Subach , Paula J. Cranfill , Michael W. Davidson , Vladislav V. Verkhusha *
1 Department of Anatomy and Structural Biology, and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, New York, New York, United States of
America, 2 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, Florida, United States of America
Abstract
Commonly used monomeric blue fluorescent proteins suffer from moderate brightness. The brightest of them, mTagBFP,
has a notably low chemical stability over time. Prolonged incubation of mTagBFP leads to its transition from a blue
fluorescent state with absorbance at 401 nm to a non-fluorescent state with absorbance at 330 nm. Here, we have
determined the chemical structure of the degraded product of the blue mTagBFP-like chromophore. On the basis of
mTagBFP we have developed an improved variant, named mTagBFP2. mTagBFP2 exhibits 2-fold greater chemical stability
and substantially higher brightness in live cells than mTagBFP. mTagBFP2 is also 1.2-fold and 1.7-fold more photostable
than mTagBFP in widefield and confocal microscopy setups, respectively. mTagBFP2 maintains all other beneficial
properties of the parental mTagBFP including the high pH stability and fast chromophore formation. The enhanced
photostability and chromophore chemical stability of mTagBFP2 make it a superior protein tag. mTagBFP2 performs well in
¨
the numerous
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