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An Engineered Split Intein for Photoactivated Protein Trans-Splicing.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Protein splicing is a natural process mediated by inteins, which catalyze the joining of protein fragments.
  • Controlling protein activity with external stimuli like light offers advanced research and therapeutic possibilities.

Purpose of the Study:

  • To engineer a synthetic photoactivatable intein (LOVInC) for light-induced protein splicing.
  • To demonstrate the broad applicability and spatial precision of LOVInC in mammalian cells.

Main Methods:

  • Engineered a synthetic intein (LOVInC) by fusing a light-sensitive LOV2 domain to a split DnaE intein.
  • Applied periodic blue light illumination to activate LOVInC-mediated protein splicing in mammalian cells.
  • Demonstrated LOVInC's ability to control the reassembly of various proteins, including fluorescent markers, RhoA, caspase-7, and GCaMP2.

Main Results:

  • Periodic blue light successfully induced protein splicing activity mediated by LOVInC in mammalian cells.
  • LOVInC enabled the light-induced reassembly of diverse target proteins, showcasing its versatility.
  • Spatial control of LOVInC activity was achieved by targeting specific mammalian cells.

Conclusions:

  • LOVInC serves as a versatile, genetically encoded platform for light-based control of protein activity.
  • This system offers precise temporal and spatial regulation of protein function in biological contexts.
  • LOVInC has broad applicability for engineering light-inducible protein systems in various research areas.