Role of helix-helix interactions in assembly of the bacteriorhodopsin lattice

Biochemistry

Volumn 38, Issue 28, 1999, Pages 9023-9030

  Isenbarger, Thomas A ^a   Krebs, Mark P ^a  

^a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; MEMBRANE PROTEIN;

ABSORPTION SPECTROSCOPY; AMINO ACID SUBSTITUTION; ARTICLE; HALOBACTERIUM SALINARUM; LIPID BILAYER; MUTAGENESIS; NONHUMAN; OLIGOMERIZATION; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; BACTERIORHODOPSINS; CIRCULAR DICHROISM; COMPUTER SIMULATION; HALOBACTERIUM SALINARUM; MEMBRANE PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; PURPLE MEMBRANE; RECOMBINANT PROTEINS;

EID: 0033551432     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9905563     Document Type: Article

References (50)

1. Gennis, R. B. (1989) Biomembranes: Molecular Structure and Function, Springer-Verlag, New York.
2. Haltia, T., and Freire, E. (1995) Biochim. Biophys. Acta 1241, 295-322.
3. Cramer, W. A., Engelman, D. M., von Heijne, G., and Rees, D. C. (1992) FASEB J. 6, 3397-3402.
4. Lemmon, M. A., MacKenzie, K. R., Arkin, I. T., and Engelman, D. M. (1997) in Membrane Protein Assembly (von Heijne, G., Ed.) pp 3-23, Chapman & Hall, New York.
5. Bormann, B. J., and Engelman, D. M. (1992) Annu. Rev. Biophys. Biomol. Struct. 21, 223-242.
6. Yeates, T. (1993) in Thermodynamics of Membrane Receptors and Channels (Jackson, M. B., Ed.) pp 1-25, CRC Press, Boca Raton, FL.
7. Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037.
8. Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. (1985) Nature 318, 618-624.
9. Kühlbrandt, W., Wang, D. N., and Fujiyoshi, Y. (1994) Nature 367, 614-621.
10. Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Nature 376, 660-669.
11. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., and Yoshikawa, S. (1996) Science 272, 1136-1144.
12. Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P., and Landau, E. M. (1997) Science 277, 1676-1681.
13. Doyle, D. A., Cabral, J. M., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., and MacKinnon, R. (1998) Science 280, 69-77.
14. Chang, G., Spencer, R. H., Lee, A. T., Barclay, M. T., and Rees, D. C. (1998) Science 282, 2220-2226.
15. Leeds, J. A., and Beckwith, J. (1998) J. Mol. Biol. 280, 799-810.
16. Langosch, D., Brosig, B., Kolmar, H., and Fritz, H. J. (1996) J. Mol. Biol. 263, 525-530.
17. Russ, W. P., and Engelman, D. M. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 863-868.
18. Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M., and Henderson, R. (1996) J. Mol. Biol. 259, 393-421.
19. Kimura, Y., Vassylyev, D. G., Miyazawa, A., Kidera, A., Matsushima, M., Mitsuoka, K., Murata, K., Hirai, T., and Fujiyoshi, Y. (1997) Nature 389, 206-211.
20. Essen, L.-O., Siegert, R., Lehmann, W. D., Oesterhelt, D. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 11673-11678.
21. Luecke, H., Richter, H. T., and Lanyi, J. K. (1998) Science 280, 1934-1937.
22. Krebs, M. P., Li, W., and Halambeck, T. P. (1997) J. Mol. Biol. 267, 172-183.
23. White, B. A. (1997) Methods Mol. Biol. 67, 173-182.
24. Krebs, M. P., Mollaaghababa, R., and Khorana, H. G. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 1987-1991.
25. Cline, S. W., and Doolittle, W. F. (1987) J. Bacteriol. 169, 1341-1344.
26. Oesterhelt, D., and Stoeckenius, W. (1974) Methods Enzymol. 31, 667-678.
27. Rehorek, M., and Heyn, M. P. (1979) Biochemistry 18, 4977-4983.
28. Cassim, J. Y. (1992) Biophys. J. 63, 1432-1442.
29. Oosawa, F., and Kasai, M. (1962) J. Mol. Biol. 4, 10-21.
30. Andreu, J. M., and Timasheff, S. N. (1986) Methods Enzymol. 130, 47-59.
31. Gulik-Krzywicki, T., Seigneuret, M., and Rigaud, J. L. (1987) J. Biol. Chem. 262, 15580-15588.
32. Weik, M., Patzelt, H., Zaccai, G., and Oesterhelt, D. (1998) Mol. Cell 1, 411-419.
33. Arkin, I. T., Adams, P. D., MacKenzie, K. R., Lemmon, M. A., Brunger, A. T., and Engelman, D. M. (1994) EMBO J. 13, 4757-4764.
34. Patricelli, M. P., Lashuel, H. A., Giang, D. K., Kelly, J. K., and Cravatt, B. F. (1998) Biochemistry 37, 15177-15187.
35. Lemmon, M. A., Flanagan, J. M., Hunt, J. F., Adair, B. D., Bormann, B. J., Dempsey, C. E., and Engelman, D. M. (1992) J. Biol. Chem. 267, 7683-7689.
36. Lemmon, M. A., Flanagan, J. M., Treutlein, H. R., Zhang, J., and Engelman, D. M. (1992) Biochemistry 31, 12719-12725.
37. Lemmon, M. A., Treutlein, H. R., Adams, P. D., Brunger, A. T., and Engelman, D. M. (1994) Nat. Struct. Biol. 1, 157-163.
38. Bogan, A. A., and Thorn, K. S. (1998) J. Mol. Biol. 280, 1-9.
39. Dall'Acqua, W., Goldman, E. R., Lin, W., Teng, C., Tsuchiya, D., Li, H., Ysern, X., Braden, B. C., Li, Y., Smith-Gill, S. J., and Mariuzza, R. A. (1998) Biochemistry 37, 7981-7991.
40. MacKenzie, K. R., and Engelman, D. M. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 3583-3590.
41. Jähnig, F. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 3691-3695.
42. Verrall, S., and Hall, Z. W. (1992) Cell 68, 23-31.
43. Phale, P. S., Philippsen, A., Kiefhaber, T., Koebnik, R., Phale, V. P., Schirmer, T., and Rosenbusch, J. P. (1998) Biochemistry 37, 15663-15670.
44. Schiffer, M., Chang, C. H., and Stevens, F. J. (1992) Protein Eng. 5, 213-214.
45. Sternberg, B., L'Hostis, C., Whiteway, C. A., and Watts, A. (1992) Biochim. Biophys. Acta 1108, 21-30.
46. Watts, A. (1995) Biophys. Chem. 55, 137-151.
47. Pearce, K. H., Jr., Ultsch, M. H., Kelley, R. F., de Vos, A. M., and Wells, J. A. (1996) Biochemistry 35, 10300-10307.
48. Brummell, D. A., Sharma, V. P., Anand, N. N., Bilous, D., Dubuc, G., Michniewicz, J., MacKenzie, C. R., Sadowska, J., Sigurskjold, B. W., Sinnott, B., Young, N. M., Bundle, D. R., and Narang, S. A. (1993) Biochemistry 32, 1180-1187.
49. Fletcher, R. (1980) Practical Methods of Optimization, Vol. 1, Wiley, New York.
50. Kraulis, P. (1991) J. Appl. Crystallogr. 24, 946-950.