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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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The mRubyFT Protein, Genetically Encoded Blue-to-Red Fluorescent Timer.

Oksana M Subach1, Aleksandr Tashkeev2, Anna V Vlaskina1

  • 1Complex of NBICS Technologies, National Research Center "Kurchatov Institute", 123182 Moscow, Russia.

International Journal of Molecular Sciences
|March 25, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed mRubyFT, a brighter blue-to-red fluorescent timer, overcoming limitations of earlier protein timers. This new tool enhances protein tracking and visualization in live cells, offering improved brightness for biological research.

Keywords:
RubyFT#11-9X-ray structurefluorescence imagingfluorescent proteingenetically encoded blue-to-red fluorescent timersmRubyFTprotein engineering

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Genetically encoded monomeric blue-to-red fluorescent timers (mFTs) are valuable for tracking protein age, trafficking, and cell labeling.
  • Existing mCherry-derived mFTs exhibit reduced brightness compared to enhanced green fluorescent protein (EGFP).

Purpose of the Study:

  • To develop a brighter blue-to-red fluorescent timer to overcome the brightness limitations of existing mFTs.
  • To characterize the properties and applications of the novel mRubyFT timer.

Main Methods:

  • Development of mRubyFT derived from mRuby2 red fluorescent protein.
  • In vitro and in vivo characterization of mRubyFT brightness, maturation time, and photoconversion efficiency.
  • Confocal imaging of cytoskeleton proteins in live mammalian cells.
  • X-ray crystallography and site-directed mutagenesis to analyze the mRubyFT structure.

Main Results:

  • mRubyFT exhibits significantly improved brightness in both blue and red forms compared to mCherry-derived Fast-FT.
  • mRubyFT demonstrates a maturation half-time of 15 hours and maximum blue form at 5.7 hours.
  • Photoconversion efficiency of mRubyFT is lower than Fast-FT, but its monomeric nature facilitates cytoskeleton labeling.
  • X-ray structure analysis revealed insights into chromophore-surrounding residues.

Conclusions:

  • mRubyFT represents a significant advancement in fluorescent timer technology, offering enhanced brightness for biological applications.
  • The improved brightness and monomeric properties of mRubyFT expand its utility in live-cell imaging and protein dynamics studies.
  • Structural analysis provides a foundation for further optimization of fluorescent timer proteins.