The Evolution of Far-Red Light Perception in Acaryochloris Marina, a Chlorophyll d-Containing Cyanobacterium

Duxbury, Zane; Willows, Robert D.; Smith, Penelope M. C.; Chen, Min

doi:10.1007/978-3-642-32034-7_139

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“…1). AM1_5894 is more closely related to BphPs from non-photosynthetic and anoxygenic photosynthetic bacteria than cyanobacterial phytochromes (Cph), based on alignment of their GAF domains40. Extending this alignment to include both the GAF and PHY domains confirms that AM1_5894 is phylogenetically separate from other Cphs and cBphPs, apart from the BphPs from another Acaryochloris ecotype, CCMEE 5410, and the filamentous cyanobacterium Leptolyngbya PCC 7375 (Figure S1).…”

Section: Resultsmentioning

confidence: 82%

“…In this work, a putative phytochrome gene, AM1_5894 , was identified in the Acaryochloris genome using BLAST and sequence analysis40. Sequence comparison revealed that AM1_5894 is part of a small cluster of cyanobacterial BphPs, which are related to BphPs from non-photosynthetic and anoxygenic photosynthetic bacteria, but distinct from the typical Cphs in Chl a -containing cyanobacteria.…”

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confidence: 99%

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Spectral properties of bacteriophytochrome AM1_5894 in the chlorophyll d-containing cyanobacterium Acaryochloris marina

Loughlin

Duxbury

Mugerwa

et al. 2016

Sci Rep

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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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Section: Resultsmentioning

confidence: 82%

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confidence: 99%