Photoconvertible Fluorescent Protein EosFP: Biophysical Properties and Cell Biology Applications

@inproceedings{Nienhaus2006PhotoconvertibleFP,
  title={Photoconvertible Fluorescent Protein EosFP: Biophysical Properties and Cell Biology Applications},
  author={G. Nienhaus and K. Nienhaus and Angela H{\"o}lzle and Sergey Ivanchenko and F. Renzi and F. Oswald and Michael Wolff and Florian Schmitt and C. R{\"o}cker and B. Vallone and W. Weidemann and R. Heilker and H. Nar and J. Wiedenmann},
  booktitle={Photochemistry and photobiology},
  year={2006}
}
Abstract EosFP is a fluorescent protein from the coral Lobophyllia hemprichii that changes its fluorescence emission from green to red upon irradiation with near-UV light. Here we present the spectroscopic properties of wild-type EosFP and a variety of monomeric and dimeric mutants and provide a structural interpretation of its oligomerization and photoconversion, which is based on X-ray structure analysis of the green and red species that we reported recently. Because functional expression of… Expand
Photoconversion of the fluorescent protein EosFP: a hybrid potential simulation study reveals intersystem crossings.
TLDR
A theoretical investigation of the photoconversion reaction in the fluorescent protein EosFP is presented, using excited-state hybrid quantum chemical and molecular mechanical potentials, in conjunction with reaction-path-finding techniques, to identify the critical role of the chromophore environment in promoting photoinduced backbone cleavage. Expand
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TLDR
This review discusses the development of advanced variants, using a structure-function based, molecular biophysics approach, of the photoactivatable fluorescent protein EosFP, which can be photoconverted from green to red fluorescence by ~400 nm light. Expand
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Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein Dendra2.
TLDR
The structure, which is very similar to those reported for the closely related proteins EosFP and Kaede, revealed a local structural change involving mainly Arg66 and a water molecule W4, which are part of a charged and hydrogen-bonded cluster of amino acids and water molecules next to the chromophore. Expand
Fluorescent proteins: maturation, photochemistry and photophysics.
  • S. Remington
  • Chemistry, Medicine
  • Current opinion in structural biology
  • 2006
It has long been appreciated that green fluorescent protein (GFP) autocatalytically forms its chromophore in a host-independent process; several of the initial steps in the reaction have recentlyExpand
Photoactivation in green to red converting EosFP and other fluorescent proteins from the GFP family
The green fluorescent protein (GFP) from the hydromedusa Aequorea victoria and its derivatives have become indispensable imaging devices in cell biology. In previous years, a wide variety of GFP-likeExpand
Rational design of photoconvertible and biphotochromic fluorescent proteins for advanced microscopy applications.
TLDR
NijiFP is presented, a promising new fluorescent protein with photoconvertible and biphotochromic properties that make it ideal for advanced fluorescence-based imaging applications and a new set of such enhanced optical highlighters derived from mEosFP and Dendra2. Expand
moxMaple3: a Photoswitchable Fluorescent Protein for PALM and Protein Highlighting in Oxidizing Cellular Environments
TLDR
The engineering of a monomeric photoswitchable FP, moxMaple3, for use in oxidizing cellular environments, especially the eukaryotic secretory pathway is described, and a point mutation to replace a cysteine substantially improved the yield of correctly folded FP capable of chromophore formation, regardless of cellular environment. Expand
Fluorescent proteins of the EosFP clade: intriguing marker tools with multiple photoactivation modes for advanced microscopy
Optical fluorescence microscopy has taken center stage in the exploration of biological structure and dynamics, especially on live specimens, and super-resolution imaging methods continue to deliverExpand
The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein.
TLDR
A model of reversible photoactivation whereby irradiation with light leads to subtle conformational changes within and around the environment of the chromophore that promotes proton transfer along an intricate polar network is proposed. Expand
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