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Dynamic Metabolons Using Stimuli-Responsive Protein Cages.

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Researchers developed dynamic protein cages to control enzyme reactions in cells. These cages can assemble and disassemble using chemical or light signals, improving biocatalysis efficiency and control.

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Area of Science:

  • Synthetic biology
  • Biochemistry
  • Protein engineering

Background:

  • Naturally evolved metabolons dynamically assemble/disassemble in response to environmental stimuli.
  • Replicating this dynamic assembly/disassembly in synthetic metabolons is challenging due to limited understanding of control mechanisms.

Purpose of the Study:

  • To synthesize chemical- and light-responsive protein cages for assembling synthetic metabolons.
  • To enable dynamic regulation of enzymatic reactions within living cells.

Main Methods:

  • Engineered protein cages with chemically responsive domains for protein recruitment.
  • Utilized light-inducible dimerization domains for optogenetic control of protein cage interactions.
  • Tethered optogenetic protein cages to membranes for spatial control of enzymatic reactions.

Main Results:

  • Chemical-induced colocalization of enzymes on protein cages enhanced specificity of branched deoxyviolacein biosynthesis by 2.6-fold.
  • Optogenetic protein cages reversibly recruited/released proteins using blue light in seconds.
  • Light-switchable, membrane-bound metabolons were formed, enabling on-demand manipulation of substrate utilization across membranes.

Conclusions:

  • Demonstrated a versatile strategy for constructing dynamic metabolons in engineered cells.
  • Enabled efficient and controllable biocatalysis through responsive protein cage systems.
  • Opened new avenues for precise control over cellular chemical reactions.