A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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-tekijät tai -toimittajat

Julkaisun tiedot

Julkaisun kaikki tekijät tai toimittajat: 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.

Lehti tai sarja: Nature Communications

eISSN: 2041-1723

Julkaisuvuosi: 2021

Volyymi: 12

Artikkelinumero: 4394

Kustantaja: Springer Science and Business Media LLC

Julkaisumaa: Britannia

Julkaisun kieli: englanti

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

Julkaisun avoin saatavuus: Avoimesti saatavilla

Julkaisukanavan avoin saatavuus: Kokonaan avoin julkaisukanava

Julkaisu on rinnakkaistallennettu (JYX): https://jyx.jyu.fi/handle/123456789/77214

Tiivistelmä

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.

Vapaat asiasanat: bacterial phytochromes; photoreceptors

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OKM-raportointi: Kyllä

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