HtrI is a dimer whose interface is sensitive to receptor photoactivation and His-166 replacements in sensory rhodopsin I

Journal of Biological Chemistry

Volumn 273, Issue 31, 1998, Pages 19722-19728

  Zhang, Xue Nong ^a   Spudich, John L ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CROSS LINKING; HALOBACTERIUM SALINARUM; OXIDATION; PHOTOACTIVATION; PHOTORECEPTOR; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; BACTERIAL PROTEINS; BACTERIORHODOPSINS; CELL MOVEMENT; CROSS-LINKING REAGENTS; DIMERIZATION; HALOBACTERIUM SALINARUM; HALORHODOPSINS; HISTIDINE; LIGHT; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOTORECEPTORS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SENSORY RHODOPSINS; SIGNAL TRANSDUCTION;

HALOBACTERIUM SALINARUM;

EID: 0032584608     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.31.19722     Document Type: Article

References (50)

1. Yao, V. J., and Spudich, J. L. (1992) Proc. Natl Acad. Sci. U. S. A. 89, 11915-11919
2. Hoff, W. D., Jung, K. H., and Spudich, J. L. (1997) Annu. Rev. Biophys. Biomol. Struct. 26, 223-258
3. Le Moual, H., and Koshland, D. E., Jr. (1996) J. Mol. Biol. 261, 568-585
4. Stock, J. B., and Surette, M. (1996) in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F., ed) 2nd Ed., pp. 123-145, American Society for Microbiology Press, Washington, D. C.
5. Falke, J. J., Bass, R. B., Butler, S. L., Chervitz, S. A., and Danielson, M. A. (1997) Annu. Rev. Cell Dev. Biol. 13, 457-512
6. Spudich, E. N., and Spudich, J. L. (1993) J. Biol. Chem. 268, 16095-16097
7. Olson, K. D., and Spudich, J. L. (1993) Biophys. J. 65, 2578-25858
8. Krah, M., Marwan, W., Vermeglio, A., and Oesterhelt, D. (1994) EMBO J. 13, 2150-2155
9. Milligan, D. L., and Koshland, D. E., Jr. (1988) J. Biol. Chem. 263, 6268-6275
10. Pakula, A. A., and Simon, M. I. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 4144-4148
11. Chervitz, S. A., and Falke, J. J. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 2545-2550
12. Hughson, A. G., and Hazelbauer, G. L. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 11546-11551
13. Milligan, D. L., and Koshland, D. E., Jr. (1991) Science 254, 1651-1654
14. Gardina, P. J., and Manson, M. D. (1996) Science 274, 425-426
15. Tatsuno, I., Homma, M., Oosawa, K., and Kawagishi, I. (1996) Science 274, 423-425
16. Chervitz, S. A., Lin, C. M., and Falke, J. J. (1995) Biochemistry 34, 9722-9733
17. Lee, G. F., Lebert, M. R., Lilly, A. A., and Hazelbauer, G. L. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 3391-3395
18. Cochran, A. G., and Kim, P. S. (1996) Science 271, 1113-1116
19. Cline, S. W., and Doolittle, W. F. (1987) J. Bacteriol. 169, 1341-1344
20. Chen, B., and Przybyla, A. E. (1994) BioTechniques 17, 657-659
21. Krebs, M. P., Spudich, E. N., Khorana, H. G., and Spudich, J. L. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 3486-3490
22. Sarkar, G., Kapelner, S., and Sommer, S. S. (1990) Nucleic Acids Res. 18, 7465
23. Boom, R., Sol, C. J. A., Salimans, M. M. M., Jansen, C. L., Wertheim-van Dillen, P. M. E., and van der Noordaa, J. (1990) J. Clin. Microbiol. 28, 495-503
24. Olson, K. D., Zhang, X. N., and Spudich, J. L. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 3185-3189
25. Lynch, B. A., and Koshland, D. E., Jr. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 10402-10406
26. Lee, G. F., Burrows, G. G., Lebert, M. R., Dutton, D. P., and Hazelbauer, G. L. (1994) J. Biol. Chem. 269, 29920-29927
27. Chervitz, S. A., and Falke, J. J. (1995) J. Biol. Chem. 270, 24043-24053
28. Perazzona, B., Spudich, E. N., and Spudich, J. L. (1996) J. Bacteriol. 178, 6475-6478
29. Jung, K. H., and Spudich, J. L. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 6557-6561
30. Zhang, X. N., and Spudich, J. L. (1997) Biophys. J. 73, 1516-1523
31. Yeh, J. I., Biemann, H. P., Prive, G. G., Pandit, J., Koshland, D. E., Jr., and Kim, S. H. (1996) J. Mol. Biol. 262, 186-201
32. Stoddard, B. L., Bui, J., and Koshland, D. E., Jr. (1992) Biochemistry 31, 11978-11983
33. Lupas, A., Van Dyke, M., and Stock, J. (1991) Science 252, 1162-1164
34. Berger, B., Wilson, D. B., Wolf, E., Tonchev, T., Milla, M., and Kim, P. S. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 8259-8263
35. Hodges, R. S. (1996) Biochem. Cell Biol. 74, 133-154
36. Lupas, A. (1996) Trends Biochem. Sci. 21, 375-382
37. McLachlan, A. D., and Stewart, M. (1975) J. Mol. Biol. 98, 293-304
38. Zhang, W., Brooun, A., Mueller, M. M., and Alam, M. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 8230-8235
39. Seidel, R., Scharf, B., Gautel, M., Kleine, K., Oesterhelt, D., and Engelhard, M. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 3036-3040
40. Zhang, W., Brooun, A., McCandless, J., Banda, P., and Alam, M. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 4649-4654
41. Chen, X., and Koshland, D. E., Jr. (1997) Biochemistry 36, 11858-11864
42. Surette, M. G., and Stock, J. B. (1996) J. Biol. Chem. 271, 17966-17973
43. Jung, K.-H., and Spudich, J. (1998) J. Bacteriol. 180, 2033-2042
44. Stoddard, B. L., Biemann, H. P., and Koshland, D. E., Jr. (1992) Cold Spring Harbor Symp. Quant. Biol. 57, 1-15
45. . Maruyama, I. N., Mikawa, Y. G., and Maruyama, H. I. (1995) J. Mol. Biol. 253, 530-546
46. Kim, S. H., Prive, G. G., Yeh, J., Scott, W. G., and Milburn, M. V. (1992) Cold Spring Harbor Symp. Quant. Biol. 57, 17-24
47. O'Shea, E. K., Klemm, J. D., Kim, P. S., and Alber, T. (1991) Science 254, 539-544
48. Hodges, R. S., Saund, A. K., Chong, P. C., St.-Pierre, S. A., and Reid R. E. (1981) J. Biol. Chem. 256, 1214-1224
49. Talbot, J. A., and Hodges, R. S. (1982) Acc. Chem. Res. 15, 224-230
50. Rost, B., and Sander, C. (1993) J. Mol. Biol. 232, 584-599