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A Prokaryotic Phytochrome Hytochrome Photoreceptors Are Almost Tive Phy Gene Product by Expression-Cloning Tively, and an Isosbestic Point at 677 Nm

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A Prokaryotic Phytochrome Hytochrome Photoreceptors Are Almost Tive Phy Gene Product by Expression-Cloning Tively, and an Isosbestic Point at 677 Nm scientific correspondence A prokaryotic phytochrome hytochrome photoreceptors are almost tive phy gene product by expression-cloning tively, and an isosbestic point at 677 nm. Pcertainly ubiquitous in green plants, in E.coli using the vector pQE1 2. This is the first report of a spectrally regulating numerous aspects of develop­ Expression of the Synechocystis PHY apo­ functional prokaryotic phytochrome. In ment throughout their life cycle. Phyto­ protein was very efficient. Products of rela­ most lower organisms light is detected by chromes were thought to exist only in tive molecular mass 85,000 accumulated to retinal or coumaric acid-based photorecep­ plants, but the recently described sequence of about 50% total soluble protein (Fig. la, lane tors. However, a Fremyella gene, rcaE, the chromosome from the cyanobacterium 1). This contrasts with results from similar involved in chromatic adaptation and Synechocystis revealed a gene that seemed to approaches with plant phytochrome genes encoding a putative histidine-kinase sensor 3 encode a phytochrome-like protein 1• By in E. coli which are usually very weakly protein was recently described' • Although expressing this gene in Escherichia coli and expressed or give rise to largely insoluble the conceptual gene product shows local feeding appropriate chromophores we show products&--10• The clone was engineered to similarities to PHYE in Arabidopsis, no sig­ that it encodes a phytochrome, which may express a C-terminal polyhistidine tag for nificant homology to the phytochrome offer an excellent starting material for crys­ nickel-affinity purification. The product chromophore-binding domain is apparent13 tallization and X-ray diffraction analysis. bound quantitatively to Ni-NTA (lane 2) and and photoreceptor activity has yet to be The carboxy-terminal amphiphilic struc­ was eluted as a homogeneous apoprotein demonstrated. The Synechocystis phy gene ture of phytochrome resembles that of (lane 3), which could be concentrated to a product is the most phytochrome-like of bacterial sensory histidine-kinases, a group 5- 10 mg rn1 - 1 solution. the Synechocystis genome and among all of enzymes used by prokaryotes to monitor Plant phytochrome apoproteins auto known prokaryotic sequences. and react to various aspects of their envir­ catalytically attach linear tetrapyrrole chro­ A simple prokaryote has advantages for onment2-4. Conceptual translation of the mophores such as phycocyanobilin (PCB)11 , basic studies of phytochrome biology. For Synechocystis sp. PCC 6803 open reading abundant in the cytoplasm of cyanobacte­ example, co-expression in the heterologous frame slr0473 (the putative Synechocystis phy ria. Indeed, the Synechocystis PHY apopro­ E. coli host might be useful in studying gene) yields a product that shows similarity tein attached purified PCB, producing subsequent components of the signal trans­ to plant phytochromes throughout its length visibly photochromic holoprotein (phy*, duction pathway. Furthermore, milligram and to bacterial sensory kinases towards the Fig. lb). In contrast, plant phytochromes amounts of homogeneous, spectrally active C terminus1•5• In particular, the chromo­ expressed in E. coli show poor autoassembly, Synechocystis phytochrome holoprotein can phore-binding domain, highly conserved in folding incorrectly8'9' 12• Synechocystis phy* be produced easily in our system. As concen­ all phytochromes, is clearly represented in was analysed spectrophotometrically after trations of 10 mg ml-' can be achieved read­ the product (residues Val 246-Asp 280). exposure to saturating monochromatic 657 ily - at least ten times higher than in other This, however, does not prove that the gene nm (red) and 731 nm (far-red) irradiation phytochrome overexpression systems known product is a genuine phytochrome. Phyco­ (Fig. le). The spectra are reminiscent of to us - there remains no barrier in principle cyanin levels prevent spectral photoreversi­ plant phytochrome-PCB adducts'' with to obtaining crystals for X-ray diffraction bility measurements6'7 of phytochrome in absorb-ance maxima at 658 and 702 nm analysis of phytochrome molecular structure. cyanobacteria, so we investigated the puta- after red and far-red irradiation, respec- Jon Hughes, Tihnan Lamparter a Franz Mittmann, Elmar Hartmann Institut fiir Pjlanzenphysiologie und Mikrobiologie, M,(K) 2 3 Freie Un iversitiit Berlin, 205- Konigin-Luise-Strasse 12- I 6, D-141 95 Berlin, Germany e-mail: [email protected] Wolfgang Gartner - Max-Planck-Institut fur Strahlenchemie, Postfach 101365, D-45413 Mulheim/Ruhr, Germany Annegret Wilde, Thomas Borner lnstitut fur Biologie, Humboldt Universitiit Berlin, Chausseestrasse 11 7, D-10115 Berlin, Germany I. Kaneko, T. et al. DNA Res. 3, l 09- 136 ( 1996). Figure I a, Expression and affinity purification 2. Schneider-Poetsch, H. A. W., Braun, B., Marx, S. & of recombinant PHY apoprotein in E. coli. SD~ Schaumburg, A. f'EBS Left. 281, 245- 249 ( 1991 ). 3. Parkinson, J. S. & Kofoid, E. C. Annu. Rev. Genet. 26, 7 1- 11 2 PAGE 10% gel stained with Coomassie. Lane l, (1992). total soluble protein in lysate; 2, after adsorption 4. Quail, P.H. t't al. Science 268, 675-680 ( 1996). to Ni-NTA matrix; 3,250 mM imidazole eluate. 5. Hughes, J., Lamparter, T. & Mittmann, F. Plant Physiol. 11 2,446 C b, Photochromicity of phy* holoprotein. ( 1996). 0.20 6. Butler, W. L., Norris, H. W., Sicgelman, H. W. & Hendricks, S. 8. of PCB were added to Stoichiometric amounts Proc. Natl Arnd. Sci. USA 45, 1703- 1708 ( 1959). Q) 0.15 PHY (3 mg m1 - '). After autoassembly (20 min in 7. Lam parter, T., Hughes, J. & Hartmann, E. Phorochem. Photobiol. () C darkness) the sample was divided and each 60, 179- 183 ( 1994). ro 0.10 .0 8. Wahleith ner, J. A. Li, L & Lagarias, J.C. Proc. Na tl Acad. Sci. 0 portion irradiated with 731 nm (far-red, left) or (J) USA 88, 10387- 1039 1 (199 1). .0 0.05 657 nm (red, right) light. Note the blue or green <( 9. lOmizawa, K.-1., Stockhaus, J., Chua, N.-H. & Furuya, M. Pfnnt 0.00 transition associated with phytochrome Cell Pliysiol. 36, 511 - 51 6 ( 199 1) . photoconversion. c, Absorbance characteristics 10. Lamparter, T ct al.}. JJ/a 11t Physiol. 147, 426-4341 ( 995). E, Palma, L.A. & Lagaria.s, J.C. -0.05 of phy* after irradiation with saturating red (R) 11. Elich, T. D., Md)onagh, A. 300 400 500 600 700 800 /. lliol. Chem. 264, 183-189 (1989). Wavelength (nm) or far-red (FR) light, and the calculated difference 12. Hill, C. et ,1/. E11 r. ]. Biod 1em. 223, 69- 77 ( 1994 ). spectrum. 13. Kehoe, D. M. & Grossman, R. Science 273, 1409-14 12 ( 1996). NATURE/ VOL 386 f 17 APRIL 1997 663 .
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