ArticleThe Journal of biological chemistry2008
Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 59 citations in OpenAlex.
- Crystal structure of the photosensory module from a PAS-less cyanobacterial phytochrome as Pr shows a mix of dark-adapted and photoactivated features.The Journal of biological chemistry · 2024Article
- Cyanobacteriochromes from Gloeobacterales Provide New Insight into the Diversification of Cyanobacterial Photoreceptors.Journal of molecular biology · 2024Article
- Vibrational Spectroscopy of Phytochromes.Biomolecules · 2023Review
- Evidence for an early green/red photocycle that precedes the diversification of GAF domain photoreceptor cyanobacteriochromes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Improved fluorescent phytochromes for in situ imaging.Scientific reports · 2022Article
- The Red Edge: Bilin-Binding Photoreceptors as Optogenetic Tools and Fluorescence Reporters.Chemical reviews · 2021Review
- Article
- Effect of the PHY Domain on the Photoisomerization Step of the Forward PChemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Structural insights into photoactivation and signalling in plant phytochromes.Nature plants · 2020Article
- Phytochrome evolution in 3D: deletion, duplication, and diversification.The New phytologist · 2020Review
- RitR is an archetype for a novel family of redox sensors in the streptococci that has evolved from two-component response regulators and is required for pneumococcal colonization.PLoS pathogens · 2018Article
- Cyanobacterial origin of plant phytochromes.Protoplasma · 2017Article
- The Crystal Structures of the N-terminal Photosensory Core Module of Agrobacterium Phytochrome Agp1 as Parallel and Anti-parallel Dimers.The Journal of biological chemistry · 2016Article
- From photon to signal in phytochromes: similarities and differences between prokaryotic and plant phytochromes.Journal of plant research · 2016Review
- Streptophyte phytochromes exhibit an N-terminus of cyanobacterial origin and a C-terminus of proteobacterial origin.BMC research notes · 2015Article
- Phytochromes: an atomic perspective on photoactivation and signaling.The Plant cell · 2014Review
- The D-ring, not the A-ring, rotates in Synechococcus OS-B' phytochrome.The Journal of biological chemistry · 2014Article
- Bright and stable near-infrared fluorescent protein for in vivo imaging.Nature biotechnology · 2011Article
- Temperature effects on Agrobacterium phytochrome Agp1.PloS one · 2011Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Photointerconversion between the red light-absorbing (Pr) form and the far-red light-absorbing (Pfr) form is the central feature that allows members of the phytochrome (Phy) superfamily to act as reversible switches in light perception. Whereas the chromophore structure and surrounding binding pocket of Pr have been described, those for Pfr have remained enigmatic for various technical reasons. Here we describe a novel pair of Phys from two thermophilic cyanobacteria, Synechococcus sp. OS-A and OS-B', that overcome several of these limitations. Like other cyanobacterial Phys, SyA-Cph1 and SyB-Cph1 covalently bind the bilin phycocyanobilin via their cGMP phosphodiesterase/adenyl cyclase/FhlA (GAF) domains and then assume the photointerconvertible Pr and Pfr states with absorption maxima at 630 and 704 nm, respectively. However, they are naturally missing the N-terminal Per/Arndt/Sim domain common to others in the Phy superfamily. Importantly, truncations containing only the GAF domain are monomeric, photochromic, and remarkably thermostable. Resonance Raman and NMR spectroscopy show that all four pyrrole ring nitrogens of phycocyanobilin are protonated both as Pr and following red light irradiation, indicating that the GAF domain by itself can complete the Pr to Pfr photocycle. (1)H-(15)N two-dimensional NMR spectra of isotopically labeled preparations of the SyB-Cph1 GAF domain revealed that a number of amino acids change their environment during photoconversion of Pr to Pfr, which can be reversed by subsequent photoconversion back to Pr. Through three-dimensional NMR spectroscopy before and after light photoexcitation, it should now be possible to define the movements of the chromophore and binding pocket during photoconversion. We also generated a series of strongly red fluorescent derivatives of SyB-Cph1, which based on their small size and thermostability may be useful as cell biological reporters.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.