A1 Journal article (refereed)
Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome (2018)


Woitowich, N. C., Halavaty, A. S., Waltz, P., Kupitz, C., Valera, J., Tracy, G., . . . Stojković, E. A. (2018). Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome. IUCrJ, 5 (5), 619-634. doi:10.1107/S2052252518010631


JYU authors or editors


Publication details

All authors or editors: Woitowich, Nicole C.; Halavaty, Andrei S.; Waltz, Patricia; Kupitz, Christopher; Valera, Joseph; Tracy, Gregory; Gallagher, Kevin D.; Claesson, Elin; Nakane, Takanori; Pandey, Suraj; et al.

Journal or series: IUCrJ

ISSN: 2052-2525

eISSN: 2052-2525

Publication year: 2018

Volume: 5

Issue number: 5

Pages range: 619-634

Publisher: International Union of Crystallography

Publication country: United Kingdom

Publication language: English

DOI: http://doi.org/10.1107/S2052252518010631

Open Access: Publication published in an open access channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/59673


Abstract

Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxo­bacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium.


Keywords: photobiology; photosynthesis; bacteria; proteins

Free keywords: phytochromes; photoreceptors; photosynthetic bacteria; myxobacteria; absorption spectra


Contributing organizations


Related projects

Biologiset fotosensorit toiminnassa - Ko
Ihalainen, Janne
Academy of Finland
01/09/2016-31/08/2020


Ministry reporting: Yes

Reporting Year: 2018

JUFO rating: 1


Last updated on 2020-18-10 at 20:05