ArticleScientific reports2016
Spectral properties of bacteriophytochrome AM1_5894 in the chlorophyll d-containing cyanobacterium Acaryochloris marina.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 18 citations in OpenAlex.
- Transcriptomic Remodeling of Light Harvesting and Photosystem Genes inPlants (Basel, Switzerland) · 2026Article
- Dual-Cys bacteriophytochromes: intermediates in cyanobacterial phytochrome evolution?The FEBS journal · 2025Article
- A genetically encoded far-red fluorescent calcium ion biosensor derived from a biliverdin-binding protein.Protein science : a publication of the Protein Society · 2022Article
- The impact of chromophore choice on the assembly kinetics and primary photochemistry of a red/green cyanobacteriochrome.Physical chemistry chemical physics : PCCP · 2021Article
- Near-Infrared Markers based on Bacterial Phytochromes with Phycocyanobilin as a Chromophore.International journal of molecular sciences · 2019Article
- Bacteriophytochromes - from informative model systems of phytochrome function to powerful tools in cell biology.Current opinion in structural biology · 2019Review
- Article
- Molecular characterization of DThe Journal of biological chemistry · 2018Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Acaryochloris marina, a unicellular oxygenic photosynthetic cyanobacterium, has uniquely adapted to far-red light-enriched environments using red-shifted chlorophyll d. To understand red-light use in Acaryochloris, the genome of this cyanobacterium was searched for red/far-red light photoreceptors from the phytochrome family, resulting in identification of a putative bacteriophytochrome AM1_5894. AM1_5894 contains three standard domains of photosensory components as well as a putative C-terminal signal transduction component consisting of a histidine kinase and receiver domain. The photosensory domains of AM1_5894 autocatalytically assemble with biliverdin in a covalent fashion. This assembled AM1_5894 shows the typical photoreversible conversion of bacterial phytochromes with a ground-state red-light absorbing (Pr) form with λBV max[Pr] 705 nm, and a red-light inducible far-red light absorbing (Pfr) form with λBV max[Pfr] 758 nm. Surprisingly, AM1_5894 also autocatalytically assembles with phycocyanobilin, involving photoreversible conversion of λPCB max[Pr] 682 nm and λPCB max[Pfr] 734 nm, respectively. Our results suggest phycocyanobilin is also covalently bound to AM1_5894, while mutation of a cysteine residue (Cys11Ser) abolishes this covalent binding. The physiological function of AM1_5894 in cyanobacteria containing red-shifted chlorophylls is discussed.
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