ArticleNature communications2021
Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 59 citations in OpenAlex.
- Phototrophicity and genomic composition in plant-associated Sphingomonas faeni strains.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026Article
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- Red-Light-Only Control of Protein-Protein Interactions Using a Cyanobacteriochrome (UNICYCL).ACS central science · 2026Article
- Detection of Histidine Kinase Activities of Bacteriophytochromes with Phos-tag™ Acrylamide Gel Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Analyzing In Vitro Autokinase Activity of Microbial Phytochromes Under Well-Defined Light Conditions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Chemical Mechanism of Allosteric and Asymmetric Dark Reversion in a Bacterial Phytochrome Uncovered by Cryo-EM.Journal of the American Chemical Society · 2025Article
- Integrating protein sequence design and evolutionary sequence conservation to uncover spectral tuning sites in red-light photoreceptors.Structure (London, England : 1993) · 2025Article
- Engineering NIR-sighted bacteria.eLife · 2025Article
- AProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Optogenetic-Controlled iPSC-Based Vaccines for Prophylactic and Therapeutic Tumor Suppression in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Untangling the Complexity of Two-Component Signal Transduction in Bacteria.Microorganisms · 2025Review
- Traits of Bathy Phytochromes and Application to Bacterial Optogenetics.ACS synthetic biology · 2025Article
- Pr and Pfr structures of plant phytochrome A.Nature communications · 2025Article
- Effects of binding partners on thermal reversion rates of photoswitchable molecules.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- ThemBio · 2025Article
- Signaling by a bacterial phytochrome histidine kinase involves a conformational cascade reorganizing the dimeric photoreceptor.Nature communications · 2024Article
- Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling.Nature communications · 2024Article
- Current Trends of Bacterial and Fungal Optoproteins for Novel Optical Applications.International journal of molecular sciences · 2023Review
- The structure of Arabidopsis phytochrome A reveals topological and functional diversification among the plant photoreceptor isoforms.Nature plants · 2023Article
- Phosphorylation chemistry of the Bordetella PlrSR TCS and its contribution to bacterial persistence in the lower respiratory tract.Molecular microbiology · 2023Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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