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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Natronobacterium

 
 
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High impact information on Natronobacterium

  • We report an atomic-resolution structure for a sensory member of the microbial rhodopsin family, the phototaxis receptor sensory rhodopsin II (NpSRII), which mediates blue-light avoidance by the haloarchaeon Natronobacterium pharaonis [1].
  • Halocyanin, a small blue copper protein, was isolated from the haloalkaliphilic archaeon Natronobacterium pharaonis [2].
  • The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins [3].
  • Natronomonas (Natronobacterium) pharaonis halorhodopsin (NpHR) is a transmembrane, seven-helix retinal protein of the archaeal bacterium and acts as an inward light-driven chloride ion pump in the membrane [4].
  • Pharaonis phoborhodopsin (ppR), also called pharaonis sensory rhodopsin II, NpSRII, is a photoreceptor of negative phototaxis in Natronomonas (Natronobacterium) pharaonis [5].
 

Biological context of Natronobacterium

 

Anatomical context of Natronobacterium

 

Associations of Natronobacterium with chemical compounds

 

Gene context of Natronobacterium

  • The blue-light receptor genes (sopII) of sensory rhodopsin (SR) II were cloned from two species, the halophilic bacteria Haloarcula vallismortis (vSR-II) and Natronobacterium pharaonis (pSR-II) [14].
  • The present study extends the infrared analysis to another archaeal rhodopsin, pharaonis phoborhodopsin (ppR; also called pharaonis sensory rhodopsin-II, psR-II), involved in the negative phototaxis of Natronobacterium pharaonis [15].
  • Cytochrome ba3 from Natronobacterium pharaonis--an archaeal four-subunit cytochrome-c-type oxidase [16].
 

Analytical, diagnostic and therapeutic context of Natronobacterium

References

  1. Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Luecke, H., Schobert, B., Lanyi, J.K., Spudich, E.N., Spudich, J.L. Science (2001) [Pubmed]
  2. The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation. Mattar, S., Scharf, B., Kent, S.B., Rodewald, K., Oesterhelt, D., Engelhard, M. J. Biol. Chem. (1994) [Pubmed]
  3. The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins. Lanyi, J.K., Duschl, A., Hatfield, G.W., May, K., Oesterhelt, D. J. Biol. Chem. (1990) [Pubmed]
  4. Disassembling and bleaching of chloride-free pharaonis halorhodopsin by octyl-beta-glucoside. Kubo, M., Sato, M., Aizawa, T., Kojima, C., Kamo, N., Mizuguchi, M., Kawano, K., Demura, M. Biochemistry (2005) [Pubmed]
  5. Correlation of the O-intermediate rate with the pKa of Asp-75 in the dark, the counterion of the Schiff base of Pharaonis phoborhodopsin (sensory rhodopsin II). Iwamoto, M., Sudo, Y., Shimono, K., Araiso, T., Kamo, N. Biophys. J. (2005) [Pubmed]
  6. Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle. Váró, G., Brown, L.S., Sasaki, J., Kandori, H., Maeda, A., Needleman, R., Lanyi, J.K. Biochemistry (1995) [Pubmed]
  7. Vibrational modes of the protonated Schiff base in pharaonis phoborhodopsin. Shimono, K., Furutani, Y., Kamo, N., Kandori, H. Biochemistry (2003) [Pubmed]
  8. Association between a photo-intermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer. Sudo, Y., Iwamoto, M., Shimono, K., Kamo, N. J. Photochem. Photobiol. B, Biol. (2002) [Pubmed]
  9. The M intermediate of Pharaonis phoborhodopsin is photoactive. Balashov, S.P., Sumi, M., Kamo, N. Biophys. J. (2000) [Pubmed]
  10. Hydrogen-bonding alterations of the protonated Schiff base and water molecule in the chloride pump of Natronobacterium pharaonis. Shibata, M., Muneda, N., Sasaki, T., Shimono, K., Kamo, N., Demura, M., Kandori, H. Biochemistry (2005) [Pubmed]
  11. Aspartate 75 mutation in sensory rhodopsin II from Natronobacterium pharaonis does not influence the production of the K-like intermediate, but strongly affects its relaxation pathway. Losi, A., Wegener, A.A., Engelhard, M., Gärtner, W., Braslavsky, S.E. Biophys. J. (2000) [Pubmed]
  12. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. Tachibana, A. FEBS Lett. (1994) [Pubmed]
  13. Coumarin and quinolone action in archaebacteria: evidence for the presence of a DNA gyrase-like enzyme. Sioud, M., Possot, O., Elie, C., Sibold, L., Forterre, P. J. Bacteriol. (1988) [Pubmed]
  14. The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II. Seidel, R., Scharf, B., Gautel, M., Kleine, K., Oesterhelt, D., Engelhard, M. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  15. Internal water molecules of pharaonis phoborhodopsin studied by low-temperature infrared spectroscopy. Kandori, H., Furutani, Y., Shimono, K., Shichida, Y., Kamo, N. Biochemistry (2001) [Pubmed]
  16. Cytochrome ba3 from Natronobacterium pharaonis--an archaeal four-subunit cytochrome-c-type oxidase. Mattar, S., Engelhard, M. Eur. J. Biochem. (1997) [Pubmed]
  17. The hydroxylamine reaction of sensory rhodopsin II: light-induced conformational alterations with C13=C14 nonisomerizable pigment. Zadok, U., Klare, J.P., Engelhard, M., Sheves, M. Biophys. J. (2005) [Pubmed]
  18. Chromophore-anion interactions in halorhodopsin from Natronobacterium pharaonis probed by time-resolved resonance Raman spectroscopy. Gerscher, S., Mylrajan, M., Hildebrandt, P., Baron, M.H., Müller, R., Engelhard, M. Biochemistry (1997) [Pubmed]
  19. Time-resolved FTIR studies of sensory rhodopsin II (NpSRII) from Natronobacterium pharaonis: implications for proton transport and receptor activation. Hein, M., Wegener, A.A., Engelhard, M., Siebert, F. Biophys. J. (2003) [Pubmed]
 
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