Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light sensing kinases that control diverse cellular functions in plants, bacteria, and fungi.1-9 Bacterial phytochromes consist of a photosensory core and a C-terminal regulatory domain.10,11 Structures of photosensory cores are reported in the resting state12-18 and conformational responses to light activation have been proposed in the vicinity of the chromophore.19-23 However, the structure of the signalling state and the mechanism of downstream signal relay through the photosensory core remain elusive. Here, we report crystal and solution structures of the resting and active states of the photosensory core of the bacteriophytochrome from Deinococcus radiodurans. The structures reveal an open and closed form of the dimeric protein for the signalling and resting state, respectively. This nanometre scale rearrangement is controlled by refolding of an evolutionarily conserved “tongue”, which is in contact with the chromophore. The findings reveal an unusual mechanism where atomic scale conformational changes around the chromophore are first amplified into an Ångström scale distance change in the tongue, and further grow into a nanometre scale conformational signal. The structural mechanism is a blueprint for understanding how the sensor proteins connect to the cellular signalling network.

Unconventional ferroelectricity exhibited by hafnia-based thin films, robust at nanoscale sizes, presents tremendous opportunities in nanoelectronics. However, the exact nature of polarization switching remains controversial. We investigated La0.67Sr0.33MnO3/Hf0.5Zr0.5O2 capacitor interfaced with various top electrodes while in situ electrical biasing using atomic resolution microscopy with direct oxygen imaging, as well as synchrotron nanobeam diffraction. When the top electrode is oxygen reactive, we clearly show reversible oxygen vacancy migration with electrodes being the source and sink of oxygen, and the dielectric layer acting as a fast conduit at millisecond timescales. With non-reactive top electrodes and at longer time scales (seconds), the dielectric layer also acts as an oxygen source/sink. Our results show that ferroelectricity in hafnia-based thin films is unmistakably intertwined to oxygen voltammetry.

Time-resolved x-ray solution scattering reveals the conformational signaling mechanism of a bacterial phytochrome.

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a template for signal transduction in sensor histidine kinases.