bioRxivBiophysicsPreprint
Turning the Fluorescent Protein Barrel into a Programmable Electrostatic Device Reveals Differential Bleaching States of the Chromophore
Abstract
Genetically encoded voltage indicators (GEVIs) based on fluorescent proteins (FPs) report membrane potential changes through voltage-driven conformational rearrangements of a voltage-sensing domain that perturb the electrostatic and hydrogen-bonding environment of a fused FP chromophore. While the chromophore is largely protected from the external environment by the FP {beta}-can, previous results suggest that this structure can also act as a programmable electrostatic grid that influences chromophore flexibility and fluorescence transition states. Here, we show that varying the external polar offset of {beta}-sheet residues flanking a chromophore-proximal position systematically reshapes fluorescence transitions, altering response polarity and kinetics. Importantly, the influence of these external residues depends strongly on the internal sidechain chemistry, revealing reciprocal coupling between {beta}-sheet electrostatics and chromophore-proximal residues. We further show that the functional effects of glutamine and asparagine substitutions at this position are strongly context-dependent and can be tuned by appropriate external polar offsets, consistent with electrostatic control of internal sidechain orientation and expanding the molecular switch repertoire. Disrupting steady-state fluorescence further revealed that the secondary component of the voltage-dependent fluorescence transition is preferentially light-sensitive and can be selectively diminished by repeated stimulation, indicating that it arises from a photophysically distinct process separable from the primary response. In addition, altering the chromophore protonation equilibrium (e.g., T65S) substantially changes response kinetics, indicating that chromophore state influences how {beta}-can electrostatics couple to fluorescence transitions. Together, these results define general programming rules by which the electrostatic grid of the FP {beta}-barrel can be tuned to control chromophore optical properties both at rest and during perturbation of the steady state.
- assay: fluorescence / live-cell microscopy
- research focus: cell signaling & trafficking
- approach: experimental assay
- Citations
- 0
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Exploiting threonine sidechains as molecular switches to modulate the fluorescence of genetically encoded biosensors
Lee Min Leong, Sang Chul Shin, … Bradley James Baker·bioRxiv·Apr 25, 2022
- Proton wires mediate the optical signal for ArcLight-type Genetically Encoded Voltage Indicators
B. E. Kang, L. M. Leong, … B. J. Baker·bioRxiv·Oct 6, 2020
- A general approach to engineer positive-going eFRET voltage indicators
Ahmed S. Abdelfattah, Rosario Valenti, … Eric R. Schreiter·Nature CommunicationsPeer-reviewed·Jul 10, 2020
- Different categories of fluorescent proteins result in GEVIs with similar characteristics
Jelena Platiša, Han Zhou, Vincent A. Pieribone·bioRxiv·May 6, 2020
- Improving the flexibility of Genetically Encoded Voltage Indicators via intermolecular FRET
Lee Min Leong, Bok Eum Kang, Bradley James Baker·Biophysical JournalPeer-reviewed·Mar 17, 2021
- Activation-pathway transitions in human voltage-gated proton channels revealed by a non-canonical fluorescent amino acid.
E. Suarez-Delgado, M. E. Orozco-Contreras, … L. D. Islas·bioRxiv·Jun 30, 2022