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 in | Scientific reports Vol. 6; no. 1; p. 27547 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
10.06.2016
Nature Publishing Group |
Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, United Kingdom. |
ISSN: | 2045-2322 2045-2322 |
DOI: | 10.1038/srep27547 |