Darkness inhibits autokinase activity of bacterial bathy phytochromes

  • Bathy phytochromes are a subclass of bacterial biliprotein photoreceptors that carry a biliverdin IXα chromophore. In contrast to prototypical phytochromes that adopt a red-light– absorbing Pr ground state, the far-red light–absorbing Pfrform is the thermally stable ground state of bathy phytochromes. Although the photobiology of bacterial phytochromes has been extensively studied since their discovery in the late 1990s, our understanding of the signal transduction process to the connected transmitter domains, which are often histidine kinases, remains insufficient. Initiated by the analysis of the bathy phytochrome PaBphP from Pseudomonas aeruginosa, we performed a systematic analysis of five different bathy phytochromes with the aim to derive a general statement on the correlation of photostate and autokinase output. While all proteins adopt different Pr/Pfr-fractions in response to red, blue, and far-red light, only darkness leads to a pure or highly enriched Pfr-form, directly correlated with the lowest level of autokinase activity. Using this information, we developed a method to quantitatively correlate the autokinase activity of phytochrome samples with well-defined stationary Pr/Pfrfractions. We demonstrate that the off-state of the phytochromes is the Pfr-form and that different Pr/Pfr-fractions enable the organisms to fine-tune their kinase output in response to a certain light environment. Furthermore, the output response is regulated by the rate of dark reversion, which differs significantly from 5 s to 50 min half-life. Overall, our study indicates that bathy phytochromes function as sensors of light and darkness, rather than red and far-red light, as originally postulated.
Metadaten
Author:Christina Huber, Merle Strack, Isabel Schultheiß, Julia Pielage, Xenia Mechler, Justin Hornbogen, Rolf Diller, Nicole Frankenberg-Dinkel
URN:urn:nbn:de:hbz:386-kluedo-84790
Parent Title (English):Journal of Biological Chemistry
Document Type:Article
Language of publication:English
Date of Publication (online):2024/03/09
Year of first Publication:2024
Publishing Institution:Rheinland-Pfälzische Technische Universität Kaiserslautern-Landau
Date of the Publication (Server):2024/11/13
Issue:300 (4)
Page Number:12
Source:10.1016/j.jbc.2024.107148
Faculties / Organisational entities:Kaiserslautern - Fachbereich Biologie
DDC-Cassification:5 Naturwissenschaften und Mathematik / 570 Biowissenschaften, Biologie
Collections:Open-Access-Publikationsfonds
Licence (German):Lizenz nach Originalpublikation