Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

Elina Multamäki, Rahul Nanekar, Dmitry Morozov, Topias Lievonen, David Golonka, Weixiao Yuan Wahlgren, Brigitte Stucki-Buchli, Jari Rossi, Vesa P. Hytönen, Sebastian Westenhoff, Janne A. Ihalainen (), Andreas Möglich and Heikki Takala ()
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Elina Multamäki: University of Helsinki
Rahul Nanekar: University of Jyvaskyla
Dmitry Morozov: University of Jyvaskyla
Topias Lievonen: University of Jyvaskyla
David Golonka: Lehrstuhl für Biochemie, Universität Bayreuth
Weixiao Yuan Wahlgren: Department of Chemistry and Molecular Biology, University of Gothenburg
Brigitte Stucki-Buchli: University of Jyvaskyla
Jari Rossi: University of Helsinki
Vesa P. Hytönen: Tampere University
Sebastian Westenhoff: Department of Chemistry and Molecular Biology, University of Gothenburg
Janne A. Ihalainen: University of Jyvaskyla
Andreas Möglich: Lehrstuhl für Biochemie, Universität Bayreuth
Heikki Takala: University of Helsinki

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: Abstract 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.

Date: 2021
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DOI: 10.1038/s41467-021-24676-7

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