Structural mechanism of signal transduction in a phytochrome histidine kinase
Wahlgren, W. Y., Claesson, E., Tuure, I., Trillo-Muyo, S., Bódizs, S., Ihalainen, J. A., Takala, H., & Westenhoff, S. (2022). Structural mechanism of signal transduction in a phytochrome histidine kinase. Nature Communications, 13, Article 7673. https://doi.org/10.1038/s41467-022-34893-3
Published inNature Communications
© The Author(s) 2022
Phytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 Å and 3.5 Å resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its tertiary domain arrangement, but the connector helices between the photosensory and the histidine kinase modules open up like a zipper, causing asymmetry and disorder in the effector domains. The structures provide a framework for atom-scale understanding of signaling in phytochromes, visualize allosteric communication over several nanometers, and suggest that disorder in the dimeric arrangement of the effector domains is important for phosphatase activity in a two-component system. The results have implications for the development of optogenetic applications. ...
PublisherNature Publishing Group
ISSN Search the Publication Forum2041-1723
Publication in research information system
MetadataShow full item record
Related funder(s)Academy of Finland
Funding program(s)Academy Research Fellow, AoF; Academy Project, AoF
Additional information about fundingS.W. acknowledges support from the European Research Council, ERC grant to Westenhoff, MolStrucDyn, 725642. This work was supported by Academy of Finland grants 332742 (J.A.I.) and 330678 (H.T.).
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