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@ARTICLE{Rllen:906364,
author = {Röllen, Katrin and Granzin, Joachim and Remeeva, Alina and
Davari, Mehdi D. and Gensch, Thomas and Nazarenko, Vera V.
and Kovalev, Kirill and Bogorodskiy, Andrey and
Borshchevskiy, Valentin and Hemmer, Stefanie and
Schwaneberg, Ulrich and Gordeliy, Valentin and Jaeger,
Karl-Erich and Batra-Safferling, Renu and Gushchin, Ivan and
Krauss, Ulrich},
title = {{T}he molecular basis of spectral tuning in blue- and
red-shifted flavin-binding fluorescent proteins},
journal = {The journal of biological chemistry},
volume = {296},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {FZJ-2022-01393},
pages = {100662 -},
year = {2021},
abstract = {Photoactive biological systems modify the optical
properties of their chromophores, known as spectral tuning.
Determining the molecular origin of spectral tuning is
instrumental for understanding the function and developing
applications of these biomolecules. Spectral tuning in
flavin-binding fluorescent proteins (FbFPs), an emerging
class of fluorescent reporters, is limited by their
dependency on protein-bound flavins, whose structure and
hence electronic properties cannot be altered by mutation. A
blue-shifted variant of the plant-derived improved light,
oxygen, voltage FbFP has been created by introducing a
lysine within the flavin-binding pocket, but the molecular
basis of this shift remains unconfirmed. We here
structurally characterize the blue-shifted improved light,
oxygen, voltage variant and construct a new blue-shifted
CagFbFP protein by introducing an analogous mutation. X-ray
structures of both proteins reveal displacement of the
lysine away from the chromophore and opening up of the
structure as instrumental for the blue shift. Site
saturation mutagenesis and high-throughput screening yielded
a red-shifted variant, and structural analysis revealed that
the lysine side chain of the blue-shifted variant is
stabilized close to the flavin by a secondary mutation,
accounting for the red shift. Thus, a single additional
mutation in a blue-shifted variant is sufficient to generate
a red-shifted FbFP. Using spectroscopy, X-ray
crystallography, and quantum mechanics molecular mechanics
calculations, we provide a firm structural and functional
understanding of spectral tuning in FbFPs. We also show that
the identified blue- and red-shifted variants allow for
two-color microscopy based on spectral separation. In
summary, the generated blue- and red-shifted variants
represent promising new tools for application in life
sciences.},
cin = {IBI-1 / IBI-7 / IBG-1},
ddc = {540},
cid = {I:(DE-Juel1)IBI-1-20200312 / I:(DE-Juel1)IBI-7-20200312 /
I:(DE-Juel1)IBG-1-20101118},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524) / 2171 - Biological and environmental resources
for sustainable use (POF4-217)},
pid = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-2171},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:33862085},
UT = {WOS:000672866400633},
doi = {10.1016/j.jbc.2021.100662},
url = {https://juser.fz-juelich.de/record/906364},
}