Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
Multamäki, E., Nanekar, R., Morozov, D., Lievonen, T., Golonka, D., Wahlgren, W. Y., Stucki-Buchli, B., Rossi, J., Hytönen, V. P., Westenhoff, S., Ihalainen, J. A., Möglich, A., & Takala, H. (2021). Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling. Nature Communications, 12, Article 4394. https://doi.org/10.1038/s41467-021-24676-7
Published inNature Communications
DisciplineNanoscience CenterFysikaalinen kemiaSolu- ja molekyylibiologiaNanoscience CenterPhysical ChemistryCell and Molecular Biology
© The Author(s) 2021
Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP as a light-sensitive phosphatase. While Agp1 binds its cognate response regulator only transiently, DrBphP does so strongly, which is rationalized at the structural level. Our data pinpoint two key residues affecting the balance between kinase and phosphatase activities, which immediately bears on photoreception and two-component signaling. The opposing output activities in two highly similar bacteriophytochromes suggest the use of light-controllable histidine kinases and phosphatases for optogenetics. ...
PublisherSpringer Science and Business Media LLC
Publication in research information system
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Related funder(s)Academy of Finland; European Commission; Jane and Aatos Erkko Foundation
Funding program(s)Academy Research Fellow, AoF; Academy Project, AoF; Foundation
The content of the publication reflects only the author’s view. The funder is not responsible for any use that may be made of the information it contains.
Additional information about fundingThis work was supported by Academy of Finland grants 285461, 330678 (H.T.), 296135, and 332742 (J.A.I.), Jane and Aatos Erkko Foundation (J.A.I.), Three-year grant 2018–2020 from the University of Helsinki (E.M. and H.T.), and Bayreuth Humboldt Centre Senior Fellowship 2020 (E.M. and H.T.). S.W. and W.W. acknowledge the European Research Council for support (grant number: 279944), and B.S.-B. acknowledges Swiss National Science Foundation (P2ZHP2_164991). D.M. acknowledge the BioExcel CoE (www.bioexcel.eu), funded by the European Union contracts H2020-INFRAEDI-02-2018-823830, H2020-EINFRA-2015-1-675728. ...
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