DOI: 10.1126/science.286.5449.2517. Bacteriophytochromes: Phytochrome-Like Photoreceptors from Nonphotosynthetic Eubacteria

Bacteriophytochromes: Phytochrome-Like Photoreceptors from Nonphotosynthetic Eubacteria

10.1126/science.286.5449.2517

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

Phytochromes are a family of photoreceptors used by green plants to entrain their development to the light environment. The distribution of these chromoproteins has been expanded beyond photoautotrophs with the discovery of phytochrome-like proteins in the nonphotosynthetic eubacteria Deinococcus radiodurans and Pseudomonas aeruginosa . Like plant phytochromes, the D. radiodurans receptor covalently binds linear tetrapyrroles autocatalytically to generate a photochromic holoprotein. However, the attachment site is distinct, using a histidine to potentially form a Schiff base linkage. Sequence homology and mutational analysis suggest that D. radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light.

Bibliography

Davis, S. J., Vener, A. V., & Vierstra, R. D. (1999). Bacteriophytochromes: Phytochrome-Like Photoreceptors from Nonphotosynthetic Eubacteria. Science, 286(5449), 2517â2520.

Authors 3

Seth J. Davis (first)
Alexander V. Vener (additional)
Richard D. Vierstra (additional)

References 25 Referenced 326

10.1126/science.7732376
; R. E. Kendrick and G. H. M. Kronenberg Photomorphogenesis in Plants (Kluwer Dordrecht Netherlands ed. 2 1994). (10.1007/978-94-011-1884-2)
Schneider-Poetsch H. A. W., Kolukisaoglu Ü., Clapham D. H., Hughes J., Lamparter T., Physiol. Plant. 102, 612 (1998). (10.1034/j.1399-3054.1998.1020417.x) / Physiol. Plant. by Schneider-Poetsch H. A. W. (1998)
Jiang Z.-Y., et al., Science 285, 406 (1999). (10.1126/science.285.5426.406) / Science by Jiang Z.-Y. (1999)
10.1038/386663a0
Lamparter T., et al., Proc. Natl. Acad. Sci. U.S.A. 93, 11792 (1997). (10.1073/pnas.94.22.11792) / Proc. Natl. Acad. Sci. U.S.A. by Lamparter T. (1997)
10.1073/pnas.95.23.13976
10.1126/science.284.5419.1539
10.1126/science.277.5331.1505
10.1126/science.273.5280.1409
J. A. Hoch and T. J. Silhavy Two-Component Signal Transduction (American Society for Microbiology Press Washington DC 1995). (10.1128/9781555818319)
BLAST searches were performed with the database available at . Sequence analysis was performed with GCG software (Madison WI) and MACBOXSHADE (Institute for Animal Health Pirbright UK).
S. J. Davis A. V. Vener R. D. Vierstra unpublished data.
Bhoo S. H., et al., J. Am. Chem. Soc. 119, 11717 (1997). (10.1021/ja972875s) / J. Am. Chem. Soc. by Bhoo S. H. (1997)
Oat phyA was purified as described [
Vierstra R. D., Quail P. H., Biochemistry 22, 2498 (1983); (10.1021/bi00279a029) / Biochemistry by Vierstra R. D. (1983)
]. DrBphP was amplified by polymerase chain reaction (PCR) from genomic DNA and ligated into pET28a + (Novagen Madison WI) for expression in Escherichia coli with an NH 2 -terminal polyhistidine tag and the recombinant protein was purified by nickel-chelate chromatography (Qiagen Valencia CA). Holo- Dr BphP was assembled with PCB and PΦΒ as described for Cph1 (4 6). Adducts were visualized by zinc-induced fluorescence of the chromoprotein following denaturing SDS-PAGE (11). Difference spectra were obtained after saturating R (660 nm) and FR (730 nm) irradiations (4).
We analyzed proteins and peptides using the API 365 LC/MS system (Perkin-Elmer Norwalk CT) with a C18 column (5 μm 1.0 mm by 150 mm) (Vydac Hesperia CA) and a 0 to 95% water-acetonitrile gradient in 0.05% trifluoroacetic acid for LC. Peptide hydrolysis was accomplished by incubating the Dr BphP holoprotein for 16 hours in the dark at ∼20°C in 70% formic acid with a 200-fold molar excess of CNBr over methionine.
Site-directed mutations were introduced by Quikchange (Stratagene La Jolla CA) for DrBphP (M259A) and by overlap-extension PCR for DrBphP (M259C) DrBphP (C289A) and DrBphP (H260A).
von Lintig J., et al., Plant J. 12, 625 (1997). (10.1046/j.1365-313X.1997.d01-16.x) / Plant J. by von Lintig J. (1997)
Lemee L., Peuchant E., Clerc M., Brunner M., Pfander H., Tetrahedron 53, 919 (1997). (10.1016/S0040-4020(96)01036-8) / Tetrahedron by Lemee L. (1997)
Deinococcus radiodurans R1 was grown at 30°C on carotenoid-free media prepared with solid complete yeast–synthetic media (Difco Detroit MI) supplemented with tryptone (5 g/liter) and glucose (1 g/liter). To create vectors to disrupt DrBphP DrBphR or both we generated a targeting plasmid (pFSI31) by inserting the Stu I–Fsp I fragment containing the chloroamphenicol acetyltransferase gene from pI3 (19) into the Eco RV site of pBS SK + (Stratagene). Sequences flanking DrBphP DrBphR or both were amplified by PCR from D. radiodurans DNA and introduced into pFSI31 so that after homologous integration the respective loci would be exactly replaced by the chloroamphenicol-resistance marker. Transformation and mutant identification was according to (19) and mutants were identified and confirmed by Southern blotting (10). Cells were irradiated with varying fluences of white light provided by a sodium lamp supplemented with fluorescent lighting. Deinoxanthin was measured spectrophotometrically following methanol extraction as described (19).
Gupta R. S., Johari V., J. Mol. Evol. 46, 716 (1998). (10.1007/PL00006352) / J. Mol. Evol. by Gupta R. S. (1998)
Gutman P. D., Fuchs P., Ouyang L., Minton K. W., J. Bacteriol. 175, 3581 (1993). (10.1128/jb.175.11.3581-3590.1993) / J. Bacteriol. by Gutman P. D. (1993)
We thank K. Minton for supplying D. radiodurans R1 and the pI3 plasmid O. White for discussions on the D. radiodurans sequence The Institute for Genomic Research and the Pseudomonas Genome Project for distributing the genomic sequences described here S. H. Bhoo and P.-S. Song for providing PCB and PΦB and A. Harms for assistance with MS. We dedicate this paper to the memory of Rudy J. Wodzinski. This work was supported by an NIH predoctoral fellowship (S.J.D.) and U.S. Department of Energy grant DE-FG02-88ER-13968 (R.D.V.).

Dates

Type	When
Created	23 years, 1 month ago (July 27, 2002, 5:42 a.m.)
Deposited	1 year, 7 months ago (Jan. 13, 2024, 4:50 a.m.)
Indexed	1 day, 3 hours ago (Sept. 3, 2025, 7:11 a.m.)
Issued	25 years, 8 months ago (Dec. 24, 1999)
Published	25 years, 8 months ago (Dec. 24, 1999)
Published Print	25 years, 8 months ago (Dec. 24, 1999)

Funders 0

None

BibTeX

@article{Davis_1999, title={Bacteriophytochromes: Phytochrome-Like Photoreceptors from Nonphotosynthetic Eubacteria}, volume={286}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.286.5449.2517}, DOI={10.1126/science.286.5449.2517}, number={5449}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Davis, Seth J. and Vener, Alexander V. and Vierstra, Richard D.}, year={1999}, month=dec, pages={2517–2520} }

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