RT Journal Article
SR Electronic
T1 Oxygen-induced chromophore degradation in the photoswitchable red fluorescent protein rsCherry
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2023.01.13.523900
DO 10.1101/2023.01.13.523900
A1 Thi Yen Hang Bui
A1 Elke De Zitter
A1 Benjamien Moeyaert
A1 Ludovic Pecqueur
A1 Bindu Y Srinivasu
A1 Anastassios Economou
A1 Marc Fontecave
A1 Luc Van Meervelt
A1 Peter Dedecker
A1 Brandán Pedre
YR 2023
UL http://biorxiv.org/content/early/2023/01/13/2023.01.13.523900.abstract
AB Reversibly switchable monomeric Cherry (rsCherry) is a photoswitchable variant of the red fluorescent protein mCherry. We report that this protein gradually and irreversibly loses its red fluorescence in the dark over a period of months at 4°C and a few days at 37°C. We also find that its ancestor, mCherry, undergoes a similar fluorescence loss but at a slower rate. X-ray crystallography and mass spectrometry reveal that this is caused by the cleavage of the p-hydroxyphenyl ring from the chromophore and the formation of two novel types of cyclic structures at the remaining chromophore moiety. Overall, our work sheds light on a new process occurring within fluorescent proteins, further adding to the chemical diversity and versatility of these molecules.Competing Interest StatementThe authors have declared no competing interest.