Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore

Seong-Hee Bhoo, Seth J. Davis, Joseph Walker, Baruch Karniol and Richard D. Vierstra ()
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Seong-Hee Bhoo: University of Wisconsin—Madison
Seth J. Davis: University of Wisconsin—Madison
Joseph Walker: University of Wisconsin—Madison
Baruch Karniol: University of Wisconsin—Madison
Richard D. Vierstra: University of Wisconsin—Madison

Nature, 2001, vol. 414, issue 6865, 776-779

Abstract: Abstract Phytochromes comprise a principal family of red/far-red light sensors in plants1. Although phytochromes were thought originally to be confined to photosynthetic organisms2,3, we have recently detected phytochrome-like proteins in two heterotrophic eubacteria, Deinococcus radiodurans and Pseudomonas aeruginosa4. Here we show that these form part of a widespread family of bacteriophytochromes (BphPs) with homology to two-component sensor histidine kinases. Whereas plant phytochromes use phytochromobilin as the chromophore, BphPs assemble with biliverdin, an immediate breakdown product of haem, to generate photochromic kinases that are modulated by red and far-red light. In some cases, a unique haem oxygenase responsible for the synthesis of biliverdin is part of the BphP operon. Co-expression of this oxygenase with a BphP apoprotein and a haem source is sufficient to assemble holo-BphP in vivo. Both their presence in many diverse bacteria and their simplified assembly with biliverdin suggest that BphPs are the progenitors of phytochrome-type photoreceptors.

Date: 2001
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DOI: 10.1038/414776a

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