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
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- European Commission
Ministry reporting: Yes
Reporting Year: 2021
JUFO rating: 3