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

Title data

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:
Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling.
In: Nature Communications. Vol. 12 (July 2021) . - No. 4394.
ISSN 2041-1723
DOI: https://doi.org/10.1038/s41467-021-24676-7

Project information

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Bacterial structural biology; Enzyme mechanisms; Kinases; X-ray crystallography
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 21 Jul 2021 09:21
Last Modified: 21 Jul 2021 10:40
URI: https://eref.uni-bayreuth.de/id/eprint/66670