Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1993 May;175(10):3096–3104. doi: 10.1128/jb.175.10.3096-3104.1993

The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein.

W W Sprenger 1, W D Hoff 1, J P Armitage 1, K J Hellingwerf 1
PMCID: PMC204631  PMID: 8491725

Abstract

The motile, alkalophilic, and extremely halophilic purple sulfur bacterium Ectothiorhodospira halophila is positively photophobotactic. This response results in the accumulation of bacteria in light spots (E. Hustede, M. Liebergesell, and H. G. Schlegel, Photochem. Photobiol. 50:809-815, 1989; D. E. McRee, J. A. Tainer, T. E. Meyer, J. Van Beeumen, M. A. Cusanovich, and E. D. Getzoff, Proc. Natl. Acad. Sci. USA 86:6533-6537, 1989; also, this work). In this study, we demonstrated that E. halophila is also negatively phototactic. Video analysis of free-swimming bacteria and the formation of cell distribution patterns as a result of light-color boundaries in an anaerobic suspension of cells revealed the existence of a repellent response toward intense (but nondamaging) blue light. In the presence of saturating background photosynthetic light, an increase in the intensity of blue light induced directional switches, whereas a decrease in intense blue light gave rise to suppression of these reversals. To our knowledge, this is the first report of a true repellent response to light in a free-swimming eubacterium, since the blue light response in Escherichia coli and Salmonella typhimurium (B. L. Taylor and D. E. Koshland, Jr., J. Bacteriol. 123:557-569, 1975), which requires an extremely high light intensity, is unlikely to be a sensory process. The wavelength dependence of this negative photoresponse was determined with narrow band pass interference filters. It showed similarity to the absorption spectrum of the photoactive yellow protein from E. halophila.

Full text

PDF
3096

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alam M., Lebert M., Oesterhelt D., Hazelbauer G. L. Methyl-accepting taxis proteins in Halobacterium halobium. EMBO J. 1989 Feb;8(2):631–639. doi: 10.1002/j.1460-2075.1989.tb03418.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bivin D. B., Stoeckenius W. Photoactive retinal pigments in haloalkaliphilic bacteria. J Gen Microbiol. 1986 Aug;132(8):2167–2177. doi: 10.1099/00221287-132-8-2167. [DOI] [PubMed] [Google Scholar]
  3. CLAYTON R. K. Studies in the phototaxis of Rhodospirillum rubrum. I. Action spectrum, growth in green light, and Weber law adherence. Arch Mikrobiol. 1953;19(2):107–124. doi: 10.1007/BF00446395. [DOI] [PubMed] [Google Scholar]
  4. Harayama S., Iino T. Phototactic response of aerobically cultivated Rhodospirillum rubrum. J Gen Microbiol. 1976 May;94(1):173–179. doi: 10.1099/00221287-94-1-173. [DOI] [PubMed] [Google Scholar]
  5. Hazelbauer G. L., Harayama S. Sensory transduction in bacterial chemotaxis. Int Rev Cytol. 1983;81:33–70. doi: 10.1016/s0074-7696(08)62334-7. [DOI] [PubMed] [Google Scholar]
  6. Hazelbauer G. L. The bacterial chemosensory system. Can J Microbiol. 1988 Apr;34(4):466–474. doi: 10.1139/m88-080. [DOI] [PubMed] [Google Scholar]
  7. Marwan W., Hegemann P., Oesterhelt D. Single photon detection by an archaebacterium. J Mol Biol. 1988 Feb 20;199(4):663–664. doi: 10.1016/0022-2836(88)90309-9. [DOI] [PubMed] [Google Scholar]
  8. McCain D. A., Amici L. A., Spudich J. L. Kinetically resolved states of the Halobacterium halobium flagellar motor switch and modulation of the switch by sensory rhodopsin I. J Bacteriol. 1987 Oct;169(10):4750–4758. doi: 10.1128/jb.169.10.4750-4758.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. McRee D. E., Tainer J. A., Meyer T. E., Van Beeumen J., Cusanovich M. A., Getzoff E. D. Crystallographic structure of a photoreceptor protein at 2.4 A resolution. Proc Natl Acad Sci U S A. 1989 Sep;86(17):6533–6537. doi: 10.1073/pnas.86.17.6533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Meyer T. E., Fitch J. C., Bartsch R. G., Tollin G., Cusanovich M. A. Soluble cytochromes and a photoactive yellow protein isolated from the moderately halophilic purple phototrophic bacterium, Rhodospirillum salexigens. Biochim Biophys Acta. 1990 Apr 26;1016(3):364–370. doi: 10.1016/0005-2728(90)90170-9. [DOI] [PubMed] [Google Scholar]
  11. Meyer T. E. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim Biophys Acta. 1985 Jan 23;806(1):175–183. doi: 10.1016/0005-2728(85)90094-5. [DOI] [PubMed] [Google Scholar]
  12. Meyer T. E., Tollin G., Causgrove T. P., Cheng P., Blankenship R. E. Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila. Biophys J. 1991 May;59(5):988–991. doi: 10.1016/S0006-3495(91)82313-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Meyer T. E., Tollin G., Hazzard J. H., Cusanovich M. A. Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery. Biophys J. 1989 Sep;56(3):559–564. doi: 10.1016/S0006-3495(89)82703-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Meyer T. E., Yakali E., Cusanovich M. A., Tollin G. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry. 1987 Jan 27;26(2):418–423. doi: 10.1021/bi00376a012. [DOI] [PubMed] [Google Scholar]
  15. Otomo J., Marwan W., Oesterhelt D., Desel H., Uhl R. Biosynthesis of the two halobacterial light sensors P480 and sensory rhodopsin and variation in gain of their signal transduction chains. J Bacteriol. 1989 Apr;171(4):2155–2159. doi: 10.1128/jb.171.4.2155-2159.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Parkinson J. S., Houts S. E. Isolation and behavior of Escherichia coli deletion mutants lacking chemotaxis functions. J Bacteriol. 1982 Jul;151(1):106–113. doi: 10.1128/jb.151.1.106-113.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Spudich E. N., Hasselbacher C. A., Spudich J. L. Methyl-accepting protein associated with bacterial sensory rhodopsin I. J Bacteriol. 1988 Sep;170(9):4280–4285. doi: 10.1128/jb.170.9.4280-4285.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Spudich J. L., Bogomolni R. A. Mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature. 1984 Dec 6;312(5994):509–513. doi: 10.1038/312509a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Spudich J. L., Bogomolni R. A. Sensory rhodopsin I: receptor activation and signal relay. J Bioenerg Biomembr. 1992 Apr;24(2):193–200. doi: 10.1007/BF00762677. [DOI] [PubMed] [Google Scholar]
  20. Spudich J. L., Bogomolni R. A. Sensory rhodopsins of halobacteria. Annu Rev Biophys Biophys Chem. 1988;17:193–215. doi: 10.1146/annurev.bb.17.060188.001205. [DOI] [PubMed] [Google Scholar]
  21. Taylor B. L., Koshland D. E., Jr Intrinsic and extrinsic light responses of Salmonella typhimurium and Escherichia coli. J Bacteriol. 1975 Aug;123(2):557–569. doi: 10.1128/jb.123.2.557-569.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tomioka H., Takahashi T., Kamo N., Kobatake Y. Flash spectrophotometric identification of a fourth rhodopsin-like pigment in Halobacterium halobium. Biochem Biophys Res Commun. 1986 Sep 14;139(2):389–395. doi: 10.1016/s0006-291x(86)80003-1. [DOI] [PubMed] [Google Scholar]
  23. Yan B., Takahashi T., Johnson R., Spudich J. L. Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: the case of sensory rhodopsin II. Biochemistry. 1991 Nov 5;30(44):10686–10692. doi: 10.1021/bi00108a012. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES