A1 Journal article (refereed)
Cryo-EM structures of a bathy phytochrome histidine kinase reveal a unique light-dependent activation mechanism (2024)

Bódizs, S., Mészáros, P., Grunewald, L., Takala, H., & Westenhoff, S. (2024). Cryo-EM structures of a bathy phytochrome histidine kinase reveal a unique light-dependent activation mechanism. Structure, 32(11), 1952-1962. https://doi.org/10.1016/j.str.2024.08.008

JYU authors or editors

Takala, Heikki

Publication details

All authors or editors: Bódizs, Szabolcs; Mészáros, Petra; Grunewald, Lukas; Takala, Heikki; Westenhoff, Sebastian

Journal or series: Structure

ISSN: 0969-2126

eISSN: 1878-4186

Publication year: 2024

Publication date: 30/08/2024

Volume: 32

Issue number: 11

Pages range: 1952-1962

Publisher: Elsevier

Publication country: United Kingdom

Publication language: English

DOI: https://doi.org/10.1016/j.str.2024.08.008

Publication open access: Openly available

Publication channel open access: Partially open access channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/97005

Web address of parallel published publication (pre-print): https://www.biorxiv.org/content/10.1101/2024.05.17.594632v1

Abstract

Phytochromes are photoreceptor proteins in plants, fungi, and bacteria. They can adopt two photochromic states with differential biochemical responses. The structural changes transducing the signal from the chromophore to the biochemical output modules are poorly understood due to challenges in capturing structures of the dynamic, full-length protein. Here, we present cryoelectron microscopy (cryo-EM) structures of the phytochrome from Pseudomonas aeruginosa (PaBphP) in its resting (Pfr) and photoactivated (Pr) state. The kinase-active Pr state has an asymmetric, dimeric structure, whereas the kinase-inactive Pfr state opens up. This behavior is different from other known phytochromes and we explain it with the unusually short connection between the photosensory and output modules. Multiple sequence alignment of this region suggests evolutionary optimization for different modes of signal transduction in sensor proteins. The results establish a new mechanism for light-sensing by phytochrome histidine kinases and provide input for the design of optogenetic phytochrome variants.

Keywords: receptors (biochemistry); phytochromes; kinases; bacteria; cryogenic electron microscopy; photochemistry; photobiology

Free keywords: structural biology; cryo-electron microscopy; Pseudomonas aeruginosa; photoreceptor; bacteriophytochrome; receptor structure-function; histidine; kinase

Fields of science: