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Science 16 July 1999:
Vol. 285. no. 5426, pp. 406 - 409
DOI: 10.1126/science.285.5426.406
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Reports

Bacterial Photoreceptor with Similarity to Photoactive Yellow Protein and Plant Phytochromes

ZeYu Jiang, 1 Lee R. Swem, 1 Brenda G. Rushing, 1 Savitha Devanathan, 2 Gordon Tollin, 2 Carl E. Bauer 1*

A phytochrome-like protein called Ppr was discovered in the purple photosynthetic bacterium Rhodospirillum centenum. Ppr has a photoactive yellow protein (PYP) amino-terminal domain, a central domain with similarity to phytochrome, and a carboxyl-terminal histidine kinase domain. Reconstitution experiments demonstrate that Ppr covalently attaches the blue light-absorbing chromophore p-hydroxycinnamic acid and that it has a photocycle that is spectrally similar to, but kinetically slower than, that of PYP. Ppr also regulates chalcone synthase gene expression in response to blue light with autophosphorylation inhibited in vitro by blue light. Phylogenetic analysis demonstrates that R. centenum Ppr may be ancestral to cyanobacterial and plant phytochromes.

1 Department of Biology, Indiana University, Jordan Hall, Bloomington, IN 47405, USA.
2 Department of Biochemistry, University of Arizona, Biosciences West Building, 1041 East Lowell Street, Post Office Box 210088, Tucson, AZ 85721, USA.
*   To whom correspondence should be addressed. E-mail: cbauer{at}bio.indiana.edu

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The histidine kinase-related domain participates in phytochrome B function but is dispensable.
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The Phytochromes, a Family of Red/Far-red Absorbing Photoreceptors.
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J. Biol. Chem. 276, 11453-11456
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Folding and signaling share the same pathway in a photoreceptor.
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