The transducer protein HtrII modulates the lifetimes of sensory rhodopsin II photointermediates

Biophysical Journal

Volumn 75, Issue 5, 1998, Pages 2435-2440

  Sasaki, Jun ^a   Spudich, John L ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; PROTEIN HTRII; RHODOPSIN; TRANSDUCIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION KINETICS; GENETIC ENGINEERING; HALOBACTERIUM SALINARUM; NONHUMAN; PHOTOCHEMISTRY; PHOTOLYSIS; PROTEIN ANALYSIS; PROTON TRANSPORT; RADIOISOTOPE DECAY; THERMODYNAMICS;

EID: 0031784239     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77687-8     Document Type: Article

References (35)

1. Balashov, S. P., E. S. Imasheva, T. G. Ebrey, N. Chen, D. R. Menick, and R. K. Crouch. 1997. Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry. 36: 8671-8676.
2. Bogomolni, R. A., and J. L. Spudich. 1987. The photochemical reactions of bacterial sensory rhodopsin. I. Flash photolysis study in the one micro-second to eight second time window. Biophys. J. 52:1071-1075.
3. Bogomolni, R. A., W. Stoeckenius, I. Szundi, E. Perozo, K. D. Olson, and J. L. Spudich. 1994. Removal of transducer HtrI allows electrogenic proton translocation by sensory rhodopsin I. Proc. Natl. Acad. Sci. USA. 91:10188-10192.
4. Bousche, O., S. Sonar, M. P. Krebs, H. G. Khorana, and K. J. Rothschild. 1992. Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185→Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay. Photochem. Photobiol. 56:1085-1095.
5. Brown, L. S., J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J. K. Lanyi. 1995. Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem. 270: 27122-27126.
6. Dioumaev, A. K., H. T. Richter, L. S. Brown, M. Tanio, S. Tuzi, H. Saitô, Y. Kimura, R. Needleman, and J. K. Lanyi. 1998. Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry. 37: 2496-2506.
7. Engelhard, M., B. Scharf, and F. Siebert. 1995. Protonation changes during the photocycle of sensory rhodopsin II from Natronobacterium pharaonis. FEBS Lett 395:195-198.
8. Falke, J. J., R. B. Bass, S. L. Butler, S. A. Chervitz, and M. A. Danielson. 1997. The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Dev. Biol 13:457-512.
9. Hoff, W. D., K.-H. Jung, and J. L. Spudich. 1997. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu. Rev. Biophys. Biomol. Struct. 26:223-258.
10. Hug, S. J., J. W. Lewis, C. M. Einterz, T. E. Thorgeirsson, and D. S. Kliger. 1990. Nanosecond photolysis of rhodopsin: evidence for a new, blue-shifted intermediate. Biochemistry. 29:1475-1485.
11. Kamikubo, H., M. Kataoka, G. Váró, T. Oka, F. Tokunaga, R. Needleman, and J. K. Lanyi. 1996. Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction. Proc. Natl. Acad. Sci. USA. 93: 1386-1390.
12. Kandori, H., Y. Yamazaki, M. Hatanaka, R. Needleman, L. S. Brown, T. H. Richter, J. K. Lanyi, and A. Maeda. 1997. Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin. Biochemistry. 36:5134-5141.
13. Krah, M., W. Marwan, A. Vermeglio, and D. Oesterhelt. 1994. Phototaxis of Halobacterium salinarium requires a signaling complex of sensory rhodopsin I and its methyl-accepting transducer HtrI. EMBO J. 13: 2150-2155.
14. Lanyi, J. K. 1997. Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272: 31209-31212.
15. Oesterhelt, D., J. Tittor, and E. Bamberg. 1992. A unifying concept for ion translocation by retinal proteins. J. Bioenerg. Biomembr. 24:181-191.
16. Olson, K. D., and J. L. Spudich. 1993. Removal of the transducer protein from sensory rhodopsin I exposes sites of proton release and uptake during the receptor photocycle. Biophys. J. 65:2578-2585.
17. 76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I. Biochemistry. 35: 6690-6696.
18. Rothschild, K. J. 1992. FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model. J. Bioenerg. Biomembr. 24:147-167.
19. Rudolph, J., N. Tolliday, C. Schmitt, S. C. Schuster, and D. Oesterhelt. 1995. Phosphorylation in halobacterial signal transduction. EMBO J. 14:4249-4257.
20. Sasaki, J., J. K. Lanyi, R. Needleman, T. Yoshizawa, and A. Maeda. 1994. Complete identification of C=O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin. Biochemistry. 33:3178-3184.
21. Sasaki, J., T. Yuzawa, H. Kandori, A. Maeda, and H. Hamaguchi. 1995. Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle. Biophys. J. 68:2073-2080.
22. Spudich, J. L. 1994. Protein-protein interaction converts a proton pump into a sensory receptor. Cell. 79:747-750.
23. Spudich, E. N., M. Sheves, G. Steinberg, and J. L. Spudich. 1997. Complexation of the signal transducing protein HtrI to sensory rhodopsin I and its effect on thermodynamics of signaling state deactivation. J. Phys. Chem. 101:109-113.
24. Spudich, E. N., and J. L. Spudich. 1993. The photochemical reactions of sensory rhodopsin I are altered by its transducer. J. Biol. Chem. 268: 16095-16097.
25. Spudich, E. N., S. A. Sundberg, D. Manor, and J. L. Spudich. 1986. Properties of a second sensory receptor protein in Halobacterium halobium. Proteins. 1:239-246.
26. 73 salt bridge. Proc. Natl. Acad. Sci. USA. 94:4960-4965.
27. Subramaniam, S., M. Gerstein, D. Oesterhelt, and R. Henderson. 1993. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12:1-8.
28. Takahashi, T., B. Yan, P. Mazur, F. Derguini, K. Nakanishi, and J. L. Spudich. 1990. Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II). Biochemistry. 29: 8467-8474.
29. Tomioka, H., T. Takahashi, N. Kamo, and Y. Kobatake. 1986. Flash spectrophotometric identification of a fourth rhodopsin-like pigment in Halobacterium halobium. Biochem. Biophys. Res. Commun. 139: 389-395.
30. Yan, B., T. Takahashi, R. Johnson, and J. L. Spudich. 1991. Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: the case of sensory rhodopsin II. Biochemistry. 30:10686-10692.
31. Yan, B., E. N. Spudich, M. Sheves, G. Steinberg, and J. L. Spudich. 1997. Complexation of the signal transducing protein HtrI to sensory rhodopsin I and its effect on thermodynamics of signaling state deactivation. J. Phys. Chem. 101:109-113.
32. Yao, V. J., and J. L. Spudich. 1992. Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I. Proc. Natl. Acad. Sci. USA. 89:11915-11919.
33. Zhang, W., A. Brooun, M. M. Mueller, and M. Alam. 1996. The primary structures of the archaeon Halobacterium salinarium blue light receptor sensory rhodopsin II and its transducer, a methyl-accepting protein. Proc. Natl. Acad. Sci. USA. 93:8230-8235.
34. Zhang, X.-N., and J. L. Spudich. 1998. HtrI is a dimer whose interface is sensitive to receptor photoactivation and His-166 replacements in sensory rhodopsin I. J. Biol. Chem. 273:19722-19728.
35. Zhu, J., E. N. Spudich, M. Alam, and J. L. Spudich. 1997. Effects of substitutions D73E, D73N, D103N and V106M on signaling and pH titration of sensory rhodopsin II. Photochem. Photobiol. 66:788-791.