TY - JOUR
T1 - Common pathway for the red chromophore formation in fluorescent proteins and chromoproteins
AU - Verkhusha, Vladislav V.
AU - Chudakov, Dmitry M.
AU - Gurskaya, Nadya G.
AU - Lukyanov, Sergey
AU - Lukyanov, Konstantin A.
N1 - Funding Information:
We thank Dr. Y. Miwa for pOSTet-7.81 vector. This work was supported in part by the grants from European Office of Aerospace Research and Development under ISTC partner project 2325 and Russian Academy of Sciences for the program “Physicochemical Biology.” V.V.V. acknowledges support from the grants NIH/NIDA DA14204-01 and INIA AA13489.
PY - 2004/6
Y1 - 2004/6
N2 - The mechanism of the chromophore maturation in members of the green fluorescent protein (GFP) family such as DsRed and other red fluorescent and chromoproteins was analyzed. The analysis indicates that the red chromophore results from a chemical transformation of the protonated form of the GFP-like chromophore, not from the anionic form, which appears to be a dead-end product. The data suggest a rational strategy to achieve the complete red chromophore maturation utilizing substitutions to favor the formation of the neutral phenol in GFP-like chromophore. Our approach to detect the neutral chromophore form expands the application of fluorescent timer proteins to faster promoter activities and more spectrally distinguishable fluorescent colors. Light sensitivity found in the DsRed neutral form, resulting in its instant transformation to the mature red chromophore, could be exploited to accelerate the fluorescence acquisition.
AB - The mechanism of the chromophore maturation in members of the green fluorescent protein (GFP) family such as DsRed and other red fluorescent and chromoproteins was analyzed. The analysis indicates that the red chromophore results from a chemical transformation of the protonated form of the GFP-like chromophore, not from the anionic form, which appears to be a dead-end product. The data suggest a rational strategy to achieve the complete red chromophore maturation utilizing substitutions to favor the formation of the neutral phenol in GFP-like chromophore. Our approach to detect the neutral chromophore form expands the application of fluorescent timer proteins to faster promoter activities and more spectrally distinguishable fluorescent colors. Light sensitivity found in the DsRed neutral form, resulting in its instant transformation to the mature red chromophore, could be exploited to accelerate the fluorescence acquisition.
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U2 - 10.1016/j.chembiol.2004.04.007
DO - 10.1016/j.chembiol.2004.04.007
M3 - Article
C2 - 15217617
AN - SCOPUS:3042691006
SN - 1074-5521
VL - 11
SP - 845
EP - 854
JO - Chemistry and Biology
JF - Chemistry and Biology
IS - 6
ER -