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Takala H, Niebling S, Berntsson O, et al. Light-induced structural changes in a monomeric bacteriophytochrome. Struct Dyn. 2016;3(5):054701doi: 10.1063/1.4961911.
Takala, H., Niebling, S., Berntsson, O., Björling, A., Lehtivuori, H., Häkkänen, H., Panman, M., Gustavsson, E., Hoernke, M., Newby, G., Zontone, F., Wulff, M., Menzel, A., Ihalainen, J. A., & Westenhoff, S. (2016). Light-induced structural changes in a monomeric bacteriophytochrome. Structural dynamics (Melville, N.Y.), 3(5), 054701. https://doi.org/10.1063/1.4961911
Takala, Heikki, et al. "Light-induced structural changes in a monomeric bacteriophytochrome." Structural dynamics (Melville, N.Y.) vol. 3,5 (2016): 054701. doi: https://doi.org/10.1063/1.4961911
Takala H, Niebling S, Berntsson O, Björling A, Lehtivuori H, Häkkänen H, Panman M, Gustavsson E, Hoernke M, Newby G, Zontone F, Wulff M, Menzel A, Ihalainen JA, Westenhoff S. Light-induced structural changes in a monomeric bacteriophytochrome. Struct Dyn. 2016 Aug 29;3(5):054701. doi: 10.1063/1.4961911. eCollection 2016 Sep. PMID: 27679804; PMCID: PMC5010554.
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Struct Dyn. 2016 Aug 29;3(5):054701. doi: 10.1063/1.4961911. eCollection 2016 Sep.

Light-induced structural changes in a monomeric bacteriophytochrome.

Structural dynamics (Melville, N.Y.)

Heikki Takala, Stephan Niebling, Oskar Berntsson, Alexander Björling, Heli Lehtivuori, Heikki Häkkänen, Matthijs Panman, Emil Gustavsson, Maria Hoernke, Gemma Newby, Federico Zontone, Michael Wulff, Andreas Menzel, Janne A Ihalainen, Sebastian Westenhoff

Affiliations

  1. Department of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
  2. Nanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla , Jyväskylä 40014, Finland.
  3. ESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
  4. Paul Scherrer Institut , 5232 Villigen PSI, Switzerland.

PMID: 27679804 PMCID: PMC5010554 DOI: 10.1063/1.4961911

Abstract

Phytochromes sense red light in plants and various microorganism. Light absorption causes structural changes within the protein, which alter its biochemical activity. Bacterial phytochromes are dimeric proteins, but the functional relevance of this arrangement remains unclear. Here, we use time-resolved X-ray scattering to reveal the solution structural change of a monomeric variant of the photosensory core module of the phytochrome from Deinococcus radiodurans. The data reveal two motions, a bend and a twist of the PHY domain with respect to the chromophore-binding domains. Infrared spectroscopy shows the refolding of the PHY tongue. We conclude that a monomer of the phytochrome photosensory core is sufficient to perform the light-induced structural changes. This implies that allosteric cooperation with the other monomer is not needed for structural activation. The dimeric arrangement may instead be intrinsic to the biochemical output domains of bacterial phytochromes.

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