Detection of a conserved α-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning

Journal of Biological Chemistry

Volumn 273, Issue 39, 1998, Pages 25006-25014

  Bass, Randal B ^a   Falke, Joseph J ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RECEPTOR; ASPARTIC ACID;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; SALMONELLA TYPHIMURIUM; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION;

ASPARTIC ACID; BACTERIAL PROTEINS; CHEMOTAXIS; CYSTEINE; CYTOPLASM; DISULFIDES; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; PROTEIN KINASES; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, AMINO ACID; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0032566732     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.39.25006     Document Type: Article

References (72)

1. Milburn, M. V., Prive, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E., Jr., and Kim, S. H. (1991) Science 254, 1342-1347
2. 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
3. Wurgler-Murphy, S. M., and Saito, H. (1997) Trends Biochem. Sci. 22, 172-176
4. Stock, J. B., and Surette, M. G. (1996) in Escherichia coli and Salmonella Cellular and Molecular Biology (Neidhardt, F. C., ed) pp. 1103-1129, American Society for Microbiology Press, Washington, D. C.
5. Stock, A. M., and Mowbray, S. L. (1995) Curr. Opin. Struct. Biol. 5, 744-751
6. Blair, D. F. (1995) Annu. Rev. Microbiol. 49, 489-522
7. Swanson, R. V., and Simon, M. I. (1994) Curr. Biol. 4, 234-237
8. Bray, D., Bourret, R. B., and Simon, M. I. (1993) Mol. Biol. Cell 4, 469-482
9. Parkinson, J. S. (1993) Cell 73, 857-871
10. Gegner, J. A., Graham, D. R., Roth, A. F., and Dahlquist, F. W. (1992) Cell 70, 975-982
11. Schuster, S. C., Swanson, R. V., Alex, L. A., Bourret, R. B., and Simon, M. I. (1993) Nature 365, 343-347
12. Borkovich, K. A., Kaplan, N., Hess, J. F., and Simon, M. I. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 1208-1212
13. Ninfa, E. G., Stock, A. M., Mowbray, S. L., and Stock, J. B. (1991) J. Biol. Chem. 266, 9764-9770
14. Barak, R., and Eisenbach, M. (1992) Biochemistry 31, 1821-1826
15. Kehry, M. R., Doak, T. G., and Dahlquist, F. W. (1985) J. Bacteriol. 163, 983-990
16. Russell, C. B., Stewart, R. C., and Dahlquist, F. W. (1989) J. Bacteriol. 171, 3609-3618
17. Hess, J. F., Oosawa, K., Kaplan, N., and Simon, M. I. (1988) Cell 53, 79-87
18. Danielson, M. A. (1997) The Molecular Mechanism of Transmembrane Signaling and Kinase Regulation by the Aspartate Receptor of Bacterial Chemotaxis, Ph.D. thesis, University of Colorado, Boulder, CO
19. Le Moual, H., and Koshland, D. E., Jr. (1996) J. Mol. Biol. 261, 568-585
20. Zhulin, I. B., Johnson, M. S., and Taylor, B. L. (1997) Biosci. Rep. 17, 335-342
21. Sundberg, S, A., Bogomolni, R. A., and Spudich, J. L. (1985) J. Bacteriol. 164, 282-287
22. Egger, L. A., Park, H., and Inouye, M. (1997) Genes Cells 2, 167-184
23. Nara, T., Kawagishi, I., Nishiyama, S., Homma, M., and Imae, Y. (1996) J. Biol. Chem. 271, 17932-17936
24. Iwama, T., Homma, M., and Kawagishi, I. (1997) J. Biol. Chem. 272, 13810-13815
25. Nishiyama, S., Nara, T., Homma, M., Imae, Y., and Kawagishi, I. (1997) J. Bacteriol. 179, 6573-6580
26. Baumgartner, J. W., Kim, C., Brissette, R. E., Inouye, M., Park, C., and Hazelbauer, G. L. (1994) J. Bacteriol. 176, 1157-1163
27. Krikos, A., Conley, M. P., Boyd, A., Berg. H. C., and Simon, M. I. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 1326-1330
28. Utsumi, R., Brissette, R. E., Rampersaud, A., Forst, S. A., Oosawa, K., and Inouye, M. (1989) Science 245, 1246-1249
29. Tatsuno, I., Lee, L., Kawagishi, I., Homma, M., and Imae, Y. (1994) Mol. Microbiol. 14, 755-762
30. Biemann, H.-P., Harmer, S. L., and Koshland, D. E., Jr. (1996) J. Biol. Chem. 271, 27927-27930
31. Moe, G. R., Bollag, E., and Koshland, D. E., Jr. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 5683-5687
32. Milligan, D. L., and Koshland, D. E., Jr. (1988) J. Biol. Chem. 263, 6268-6275
33. Chervitz, S. A., Lin, C. M., and Falke, J. J. (1995) Biochemistry 34, 9722-9733
34. Chervitz, S. A., and Falke, J. J. (1995) J. Biol. Chem. 270, 24043-24053
35. Falke, J. J., and Koshland, D. E., Jr. (1987) Science 237, 1596-1600
36. Pakula, A. A., and Simon, M. I. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 4144-4148
37. Lee, G. F., Burrows, G. G., Lebert, M. R., Dutton, D. P., and Hazelbauer, G. L. (1994) J. Biol. Chem. 269, 29920-29927
38. Lee, G. F., Dutton, D. P., and Hazelbauer, G. L. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 5416-5420
39. Hughson, A. G., and Hazelbauer, G. L. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 11546-11551
40. Maruyama, I. N., Mikawa, Y. G., and Maruyama, H. I. (1995) J. Mol. Biol. 253, 530-546
41. Falke, J. J., Sternberg, D. W., and Koshland, D. E., Jr. (1986) Biophys. J. 49, 20-25
42. Falke, J. J., Dernburg, A. F., Sternburg, D. A., Zalkin, N., Milligan, D. L., and Koshland, D. E. J. (1988) J. Biol. Chem. 263, 14850-14858
43. Chervitz, S. A., and Falke, J. J. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 2545-2550
44. Hughson, A. G., Lee, G. F., and Hazelbauer, G. L. (1997) Protein Sci. 6, 315-322
45. Ottemann, K. M., Thorgeirsson, T. E., Kolodziej, A. F., Shin, Y. K., and Koshland, D. E., Jr. (1998) Biochemistry 37, 7062-7069
46. Seeley, S. K., Weis, R. M., and Thompson, L. K. (1996) Biochemistry 35, 5199-5206
47. Long, D. G., and Weis, R. M. (1992) Biochemistry 31, 9904-9911
48. Mowbray, S. L., Foster, D. L., and Koshland, D. E., Jr. (1985) J. Biol. Chem. 260, 11711-11718
49. Terwilliger, T. C., and Koshland, D. E., Jr. (1984) J. Biol. Chem. 259, 7719-7725
50. Lupas, A., and Stock, J. B. (1989) J. Biol. Chem. 264, 17337-17342
51. Wu, J., Li, J., Li, G., Long, D. G., and Weis, R. M. (1996) Biochemistry 35, 4984-4993
52. Okumura, H., Nishiyama, S., Sasaki, A., Homma, M., and Kawagishi, I. (1998) J. Bacteriol. 180, 1862-1868
53. Ames, P., Yu, Y. A., and Parkinson, J. S. (1996) Mol. Microbiol. 19, 737-746
54. Ames, P., and Parkinson, J. S. (1994) J. Bacteriol. 176, 6340-6348
55. Surette, M. G., and Stock, J. B. (1996) J. Biol. Chem. 271, 17966-17973
56. Surette, M. G., Levit, M., Liu, Y., Lukat, G., Ninfa, E. G., Ninfa, A., and Stock, J. B. (1996) J. Biol. Chem. 271, 939-945
57. Danielson, M. A., Bass, R. B., and Falke, J. J. (1997) J. Biol. Chem. 272, 32878-32888
58. Butler, S. L., and Falke, J. J. (1998) Biochemistry 37, 10746-10756
59. Chen, X., and Koshland, D. E., Jr. (1997) Biochemistry 36, 11858-11864
60. Liu, J. D., and Parkinson, J. S. (1991) J. Bacteriol. 173, 4941-4951
61. Ames, P., and Parkinson, J. S. (1988) Cell 55, 817-826
62. Akabas, M. H., Stauffer, D. A., Xu, M., and Karlin, A. (1992) Science 258, 307-310
63. Frillingos, S., Sun, J., Gonzalez, A., and Kaback, H. R. (1997) Biochemistry 36, 269-273
64. Liu, J. D., and Parkinson, J. S. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 8703-8707
65. Kunkel, T. A., Bebenek, K., and McClary, J. (1991) Methods Enzymol. 204, 125-139
66. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467
67. Vogel, H. J., and Bonner, D. M. (1956) J. Biol. Chem. 218, 97-106
68. Laemmli, U. K. (1970) Nature 227, 680-685
69. Adler, J. (1966) Science 153, 708-716
70. Chelsky, D., Gutterson, N. I., and Koshland, D. E., Jr. (1984) Anal. Biochem. 141, 143-148
71. Richards, F. M. (1977) Annu. Rev. Biophys. Bioeng. 6, 151-176
72. Bogonez, E., and Koshland, D. E., Jr. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 4891-4895