A1 Journal article (refereed)
Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling (2021)

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

JYU authors or editors

Publication details

All authors or editors: Multamäki, Elina; Nanekar, Rahul; Morozov, Dmitry; Lievonen, Topias; Golonka, David; Wahlgren, Weixiao Yuan; Stucki-Buchli, Brigitte; Rossi, Jari; Hytönen, Vesa P.; Westenhoff, Sebastian; et al.

Journal or series: Nature Communications

eISSN: 2041-1723

Publication year: 2021

Publication date: 20/07/2021

Volume: 12

Article number: 4394

Publisher: Springer Science and Business Media LLC

Publication country: United Kingdom

Publication language: English

DOI: https://doi.org/10.1038/s41467-021-24676-7

Publication open access: Openly available

Publication channel open access: Open Access channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/77214

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.

Free keywords: bacterial phytochromes; photoreceptors

Contributing organizations

Related projects

Ministry reporting: Yes

Reporting Year: 2021

JUFO rating: 3