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

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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 , vol. 12 , no. 1 , 4394 . https://doi.org/10.1038/s41467-021-24676-7

Title: Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
Author: Multamäki, Elina; Nanekar, Rahul; Morozov, Dmitry; Lievonen, Topias; Golonka, David; Wahlgren, Weixiao Yuan; Stucki-Buchli, Brigitte; Rossi, Jari; Hytönen, Vesa P.; Westenhoff, Sebastian; Ihalainen, Janne A.; Möglich, Andreas; Takala, Heikki
Other contributor: University of Helsinki, Department of Anatomy
University of Helsinki, University of Jyväskylä
University of Helsinki, Staff Services
University of Helsinki, Medicum




Date: 2021-07-20
Language: eng
Number of pages: 14
Belongs to series: Nature Communications
ISSN: 2041-1723
DOI: https://doi.org/10.1038/s41467-021-24676-7
URI: http://hdl.handle.net/10138/334399
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. The bacteriophytochrome DrBphP from Deinococcus radiodurans shows high sequence homology to the histidine kinase Agp1 from Agrobacterium fabrum but lacks kinase activity. Here, the authors structurally and biochemically analyse DrBphP and Agp1, showing that DrBphP is a light-activatable phosphatase.
Subject: CYANOBACTERIAL PHYTOCHROME CPH1
HISTIDINE KINASES
AGROBACTERIUM-TUMEFACIENS
CRYSTAL-STRUCTURE
TRANSDUCTION
PROTEINS
INSIGHTS
PHOSPHORYLATION
REARRANGEMENTS
ACTIVATION
3111 Biomedicine
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