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Sci Rep. 2017 May 3;7(1):1385. doi: 10.1038/s41598-017-01497-7.

Blue-light reception through quaternary transitions.

Author information

1
Fachbereich Physik, Institut für Experimentalphysik, Freie Universität Berlin, 14195, Berlin, Germany.
2
Biophysikalische Chemie, Institut für Biologie, Humboldt-Universität zu Berlin, 10115, Berlin, Germany.
3
Biophysikalische Chemie, Institut für Biologie, Humboldt-Universität zu Berlin, 10115, Berlin, Germany. andreas.moeglich@uni-bayreuth.de.
4
Lehrstuhl für Biochemie and Research Center for Bio-Macromolecules, Universität Bayreuth, 95440, Bayreuth, Germany. andreas.moeglich@uni-bayreuth.de.
5
Fachbereich Physik, Institut für Experimentalphysik, Freie Universität Berlin, 14195, Berlin, Germany. robert.bittl@fu-berlin.de.

Abstract

Sensory photoreceptors absorb light via their photosensor modules and trigger downstream physiological adaptations via their effector modules. Light reception accordingly depends on precisely orchestrated interactions between these modules, the molecular details of which often remain elusive. Using electron-electron double resonance (ELDOR) spectroscopy and site-directed spin labelling, we chart the structural transitions facilitating blue-light reception in the engineered light-oxygen-voltage (LOV) histidine kinase YF1 which represents a paradigm for numerous natural signal receptors. Structural modelling based on pair-wise distance constraints derived from ELDOR pinpoint light-induced rotation and splaying apart of the two LOV photosensors in the dimeric photoreceptor. Resultant molecular strain likely relaxes as left-handed supercoiling of the coiled-coil linker connecting sensor and effector units. ELDOR data on a photoreceptor variant with an inverted signal response indicate a drastically altered dimer interface but light-induced structural transitions in the linker that are similar to those in YF1. Taken together, we provide mechanistic insight into the signal trajectories of LOV photoreceptors and histidine kinases that inform molecular simulations and the engineering of novel receptors.

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