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

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 photoreceptor...

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Published inScientific reports Vol. 6; no. 1; p. 27547
Main Authors Loughlin, Patrick C., Duxbury, Zane, Mugerwa, Tendo T. Mukasa, Smith, Penelope M. C., Willows, Robert D., Chen, Min
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 10.06.2016
Nature Publishing Group
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Summary: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 λ BV max [Pr] 705 nm, and a red-light inducible far-red light absorbing (Pfr) form with λ BV max [Pfr] 758 nm. Surprisingly, AM1_5894 also autocatalytically assembles with phycocyanobilin, involving photoreversible conversion of λ PCB max [Pr] 682 nm and λ PCB 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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Present address: The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep27547