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Harnessing phytochrome's glowing potential.

Amanda J Fischer1, J Clark Lagarias

  • 1Section of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 19, 2004
PubMed
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Directed evolution transformed a cyanobacterial phytochrome into a red fluorescent biliprotein by altering its prosthetic group. This discovery offers new fluorescent protein tools for near-infrared biological imaging.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Phytochromes are photoreceptors controlling light sensing in plants and bacteria.
  • Their function relies on a linear tetrapyrrole prosthetic group within an apoprotein.
  • Understanding phytochrome structure-function is key to developing novel optical tools.

Purpose of the Study:

  • To investigate the structural basis of cyanobacterial phytochrome light sensory activity.
  • To remodel the prosthetic group's chemical environment through directed evolution.
  • To create novel fluorescent biliproteins for biological applications.

Main Methods:

  • Directed evolution of a cyanobacterial phytochrome.
  • Site-directed mutagenesis, specifically tyrosine-to-histidine substitutions.

Related Experiment Videos

  • Spectroscopic analysis to characterize photophysical properties.

    • Main Results:

    • Identified a critical apoprotein region for native spectroscopic properties.
    • Discovered a tyrosine-to-histidine mutation yielding an intensely red fluorescent biliprotein.
    • The mutated phytochrome exhibits unique spectral characteristics.

    Conclusions:

    • A conserved tyrosine residue is crucial for phytochrome photochemistry.
    • Engineered fluorescent phytochromes can serve as novel near-infrared probes.
    • This work expands the toolkit of genetically encoded fluorescent proteins.