Abstract
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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acyltransferases / genetics
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Amino Acid Sequence
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Apoproteins / chemistry
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Apoproteins / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology
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Chemotaxis
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Cloning, Molecular
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Coumaric Acids / metabolism
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Gene Expression Regulation, Bacterial
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Histidine Kinase
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Light
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Molecular Sequence Data
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Mutation
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Phosphorylation
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Photoreceptors, Microbial*
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Phylogeny
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Phytochrome / chemistry*
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Propionates
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Protein Kinases / metabolism
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Rhodospirillum / chemistry*
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Rhodospirillum / genetics
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Rhodospirillum / physiology
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Sequence Alignment
Substances
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Apoproteins
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Bacterial Proteins
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Coumaric Acids
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Photoreceptors, Microbial
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Ppr protein, Rhodospirillum centenum
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Propionates
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photoactive yellow protein, Bacteria
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Phytochrome
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Acyltransferases
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flavanone synthetase
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Protein Kinases
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Histidine Kinase
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p-coumaric acid