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Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore

Nature volume 414, pages 776779 (13 December 2001) | Download Citation

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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.

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Acknowledgements

We thank P.-S. Song for providing PCB and PEB, and M. Wexler, J. Todd and A. Johnston for making the R. leguminosarium sequences available before publication. This work was supported by grants from the US Department of Energy and the National Science Foundation to R.D.V.

Author information

Author notes

    • Seong-Hee Bhoo
    •  & Seth J. Davis

    These authors contributed equally to this work

    • Seth J. Davis

    Present address: Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.

Affiliations

  1. *Cellular and Molecular Biology Program and the Department of Horticulture, University of Wisconsin—Madison, 1575 Linden Drive, Madison, Wisconsin 53706, USA

    • Seong-Hee Bhoo
    • , Seth J. Davis
    • , Joseph Walker
    • , Baruch Karniol
    •  & Richard D. Vierstra

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The authors declare no competing financial interests.

Corresponding author

Correspondence to Richard D. Vierstra.

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https://doi.org/10.1038/414776a

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