Thermal Denaturation of the Na,K-ATPase Provides Evidence for α-α Oligomeric Interaction and γ Subunit Association with the C-terminal Domain

Journal of Biological Chemistry

Volumn 276, Issue 10, 2001, Pages 7357-7365

  Donnet, Claudia ^a   Arystarkhova, Elena ^a   Sweadner, Kathleen J ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOLOGICAL MEMBRANES; DIMERS; STRUCTURE (COMPOSITION); THERMODYNAMIC STABILITY;

THERMAL DENATURATION;

PROTEINS;

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); DODECYL SULFATE SODIUM; OLIGOMER; PROTEINASE; TRYPSIN; GLUTAMYL ENDOPEPTIDASE; ISOPROTEIN; SERINE PROTEINASE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOPLASM; DISSOCIATION; DOG; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME SUBUNIT; HEATING; KIDNEY MEDULLA; KIDNEY MICROSOME; LIPID BILAYER; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SWINE; ANIMAL; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; HEAT; KIDNEY; METABOLISM; MOUSE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; RAT; TEMPERATURE;

ANIMALIA; CANIS FAMILIARIS; HYLOBATIDAE; SUS SCROFA;

ANIMALS; CYTOPLASM; DIMERIZATION; DOGS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HEAT; KIDNEY; LIPID BILAYERS; MICE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NA(+)-K(+)-EXCHANGING ATPASE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; SERINE ENDOPEPTIDASES; SWINE; TEMPERATURE; TRYPSIN;

EID: 0035831504     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M009131200     Document Type: Article

References (65)

1. Møller, J. V., Juul, B., and le Maire, M. (1996) Biochim. Biophys. Acta 1286, 1-51
2. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647-655
3. Chow, D. C., and Forte, J. G. (1995) J. Exp. Biol. 198, 1-17
4. Therien, A. G., and Blostein, R. (2000) Am. J. Physiol. 279, C541-C566
5. Arystarkhova, E., Wetzel, R. K., Asinovski, N. K., and Sweadner, K. J. (1999) J. Biol. Chem. 274, 33183-33185
6. Beguin, P., Wang, X., Firsov, D., Puoti, A., Claeys, D., Horisberger, J. D., and Geering, K. (1997) EMBO J. 16, 4250-4260
7. Arystarkhova, E., Wetzel, R. K., Asinovski, N. K., and Sweadner, K. J. (2000) in Na/K-ATPase and Related ATPases (Taniguchi, K. and Kaya, S., eds) pp. 489-496, Elsevier, Amsterdam
8. Or, E., Goldshleger, R., Tal, D. M., and Karlish, S. J. D. (1996) Biochemistry 35, 6853-6864
9. Haltia, T., and Freire, E. (1995) Biochim. Biophys. Acta 1241, 295-322
10. Lemmon, M. A., and Engelman, D. M. (1994) Q. Rev. Biophys. 27, 157-218
11. Arystarkhova, E., Gibbons, D. L., and Sweadner, K. J. (1995) J. Biol. Chem. 270, 8785-8796
12. Goldshleger, R., Tal, D. M., and Karlish, S. J. D. (1995) Biochemistry 34, 8668-8679
13. Jørgensen, P. L. (1988) Methods Enzymol. 156, 29-43
14. Esmann, M. (1988) Methods Enzymol. 156, 105-115
15. Weber, K., Pringle, J. R., and Osborn, M. (1972) Methods Enzymol. 26, 3-27
16. Schagger, H., and von Jagow, G. (1987) Anal. Biochem. 166, 368-379
17. Jørgensen, P. L., and Collins, J. H. (1986) Biochim. Biophys. Acta 860, 570-576
18. Sweadner, K. J. (1991) Anal. Biochem. 194, 130-135
19. Arystarkhova, E., and Sweadner, K. J. (1996) J. Biol. Chem. 271, 23407-23417
20. Cleveland, D. W., Fischer, S. G., Kirschner, M. W., and Laemmli, U. K. (1977) J. Biol. Chem. 252, 1102-1106
21. Felsenfeld, D. P., and Sweadner, K. J. (1988) J. Biol. Chem. 263, 10932-10942
22. Therien, A. G., Goldshleger, R., Karlish, S. J. D., and Blostein, R. (1997) J. Biol. Chem. 272, 32624-32628
23. Shainskaya, A., and Karlish, S. J. D. (1994) J. Biol. Chem. 269, 10780-10789
24. Hu, Y.-K., and Kaplan, J. H. (2000) J. Biol. Chem. 275, 19185-19191
25. Sarvazyan, N. A., Ivanov, A., Modyanov, N. N., and Askari, A. (1997) J. Biol. Chem. 272, 7855-7858
26. Or, E., Goldshleger, R., and Karlish, S. J. D. (1999) J. Biol. Chem. 274, 2802-2809
27. Besancon, M., Shin, J. M., Mercier, F., Munson, K., Miller, M., Hersey, S., and Sachs, G. (1993) Biochemistry 32, 2345-2355
28. Shin, J. S., Kajimura, M., Arguello, J. M., Kaplan, J. H., and Sachs, G. (1994) J. Biochem. 269, 22533-22537
29. Møller, J. V., Ning, G., Maunsbach, A. B., Fujimoto, K., Asai, K., Juul, B., Lee, Y.-J., Gomez de Gracia, A., Falson, P., and le Maire, M. (1997) J. Biol. Chem. 272, 29015-29032
30. Gasset, M., Laynez, J., Menendez, M., Raussens, V., and Goormaghtigh, E. (1997) J. Biol. Chem. 272, 1608-1614
31. Jørgensen, P. L., and Andersen, J. P. (1986) Biochemistry 25, 2889-2897
32. Rabon, E. C., Smillie, K., Seru, V., and Rabon, R. (1993) J. Biol. Chem. 268, 8012-8018
33. Karlish, S. J. D., Goldshleger, R., and Stein, W. D. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 4566-4570
34. Heimburg, T., Esmann, M., and Marsh, D. (1997) J. Biol. Chem. 272, 25685-25692
35. Goormaghtigh, E., Vigneron, L., Scarborough, G. A., and Ruysschaert, J. M. (1994) J. Biol. Chem. 269, 27409-27413
36. Zhang, P., Toyoshima, C., Yonekura, K., Green, N. M., and Stokes, D. L. (1998) Nature 392, 835-839
37. Auer, M., Scarborough, G. A., and Kuhlbrandt, W. (1998) Nature 392, 840-843
38. Brotherus, J. R., Jacobsen, L., and Jørgensen, P. L. (1983) Biochim. Biophys. Acta 731, 290-303
39. Hayashi, Y., Mimura, K., Matsui, H., and Takagi, T. (1989) Biochim. Biophys. Acta 983, 217-229
40. Martin, D. W., Marecek, J., Scarlata, S., and Sachs, J. R. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 3195-3200
41. Askari, A., and Huang, W. (1980) Biochem. Biophys. Res. Commun. 93, 448-453
42. Periyasamy, S. M., Huang, W.-H., and Askari, A. (1983) J. Biol. Chem. 258, 9878-9885
43. Ganjeizadeh, M., Zolotarjova, N., Huang, W. H., and Askari, A. (1995) J. Biol. Chem. 270, 15707-15710
44. Mahaney, J. E., and Grisham, C. M. (1992) Biochemistry 31, 2025-2034
45. Amler, E., Abbott, A., and Ball, W. J., Jr. (1992) Biophys. J. 61, 553-568
46. Linnertz, H., Urbanova, P., Obsil, T., Herman, P., Amler, E., and Schoner, W. (1998) J. Biol. Chem. 273, 28813-28821
47. Mimura, K., Matsui, H., Takagi, T., and Hayashi, Y. (1993) Biochim. Biophys. Acta 1145, 63-74
48. Blanco, G., Koster, J. C., and Mercer, R. W. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 8542-8546
49. Froehlich, J. P., Taniguchi, K., Fendler, K., Mahoney, J. E., and Albers, R. W. (1997) Ann. N. Y. Acad. Sci. U. S. A. 834, 280-296
50. Yokoyama, T., Kaya, S., Abe, K., Taniguchi, K., Katoh, T., Yazawa, M., Hayashi, Y., and Mardh, S. (1999) J. Biol. Chem. 274, 31792-31796
51. Hebert, H., Skriver, E., Kaveus, U., and Maunsbach, A. B. (1990) FEBS Lett. 268, 83-87
52. Mohraz, M., Simpson, M. V., and Smith, P. R. (1987) J. Cell Biol. 105, 1-8
53. Sagne, C., Isambert, M.-F., Henry, J.-P., and Gasnier, B. (1996) Biochem. J. 316, 825-831
54. Brotherus, J. R., Moller, J. V., and Jørgensen, P. L. (1981) Biochem. Biophys. Res. Commun. 100, 146-154
55. Sweadner, K. J. (1990) Biochim. Biophys. Acta 1029, 13-23
56. Collins, J. H., Forbush, B., III, Lane, L. K., Ling, E., Schwartz, A., and Zot, A. (1982) Biochim. Biophys. Acta 686, 7-12
57. Sweadner, K. J., and Rael, E. (2000) Genomics 68, 41-56
58. Lutsenko, S., Anderko, R., and Kaplan, J. H. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 7936-7940
59. Shainskaya, A., Nesaty, V., and Karlish, S. J. D. (1998) J. Biol. Chem. 273, 7311-7319
60. Liu, L., and Askari, A. (1997) J. Biol. Chem. 272, 14380-14386
61. Colonna, T. E., Huynh, L., and Fambrough, D. M. (1997) J. Biol. Chem. 272, 12366-12372
62. Or, E., Goldshleger, R., Shainskaya, A., and Karlish, S. J. D. (1998) Biochemistry 37, 8197-8207
63. Ivanov, A., Zhao, H., and Modyanov, N. N. (2000) Biochemistry 39, 9778-9785
64. Sweadner, K. J., and Arystarkhova, E. (1992) Ann. N. Y. Acad. Sci. U. S. A. 671, 217-227
65. Karlish, S. J. D., Goldshleger, R., and Jørgensen, P. L. (1993) J. Biol. Chem. 268, 3471-3478