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Structural biology

Action at a distance in a light receptor

Nature volume 509, pages 174–175 (2014)Cite this article

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A tour de force of X-ray scattering has yielded structures of a phytochrome photoreceptor in its dark and illuminated states, showing how localized protein refolding magnifies a light signal to form a cellular message. See Letter p.245

Sensor proteins allow organisms to perceive and appropriately respond to environmental changes. They are molecular machines comprised of sensory domains and effector modules; a specific signal is received by the former and communicated to the latter through structural changes, creating an output activity that directs a cellular response. Phytochromes are dimeric sensor proteins that specifically absorb red and near-infrared light using a covalently tethered chromophore molecule housed in a light-sensitive (photosensory) core. In this issue, Takala et al.1 (page 245) demonstrate how visible light is interpreted and spatially magnified by the phytochrome dimer in a chain reaction that uses key features of the protein's three-dimensional structure.

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Figure 1: Signal magnification in phytochrome light sensors.

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Authors and Affiliations

  1. Anna W. Baker and Katrina T. Forest are in the Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.,

    Anna W. Baker & Katrina T. Forest

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  1. Anna W. Baker
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  2. Katrina T. Forest
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Correspondence to Anna W. Baker or Katrina T. Forest.

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Baker, A., Forest, K. Action at a distance in a light receptor. Nature 509, 174–175 (2014). https://doi.org/10.1038/nature13331

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