Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and of the ionic composition of the solution on the structure of F-actin

Biochemical Journal

Volumn 316, Issue 3, 1996, Pages 713-721

  Strzelecka Gołaszeska, Hanna ^a   Woźniak, Aleksandra ^a   Hult, Thomas ^b   Lindberg, Uno ^b  

^a NENCKI INSTITUTE OF EXPERIMENTAL BIOLOGY   (Poland)

^b STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; DEOXYRIBONUCLEASE I; DIVALENT CATION; F ACTIN; G ACTIN; MAGNESIUM ION; POTASSIUM CHLORIDE; PROTEINASE; SUBTILISIN; TRYPSIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; IONIC STRENGTH; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN STRUCTURE;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CATIONS, DIVALENT; CYSTEINE; FLUORESCENT DYES; LYSINE; MACROMOLECULAR SUBSTANCES; MAGNESIUM; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; NAPHTHALENESULFONATES; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; PROTEIN CONFORMATION; RABBITS; SOLUTIONS; SUBTILISINS; TRYPSIN;

EID: 0029847601     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3160713     Document Type: Article

References (55)

1. Oosawa, F. (1993) Biophys. Chem. 47, 101-111
2. Yanagida, T., Nakase, M., Nishiyama, K. and Oosawa, F. (1984) Nature (London) 307, 58-60
3. Prochniewicz, E. and Yanagida, T. (1990) J. Mol. Biol. 216, 761-772
4. Kwon, H., Hardwicke, P. M. D., Collins, J. H., Zhao, X. and Szent-Györgyi, A. G. (1994) J. Muscle Res. Cell Motil. 15, 555-562
5. Kojima, H., Ishijima, A. and Yanagida, T. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 12962-12966
6. Huxley, H. E., Stewart, A., Sosa, H. and Irving, T. (1994) Biophys. J. 67, 2411-2421
7. Wakabayashi, K., Sugimoto, Y. Tanaka, H., Ueno, Y., Takezawa, Y. and Amemiya, Y. (1994) Biophys. J. 67, 2422-2435
8. Asakura, S., Taniguchi, M. and Oosawa, F. (1963) J. Mol. Biol. 7, 55-69
9. Oosawa, F. (1983) in Muscle and Nonmuscle Motility (Stracher, A., ed.), vol. 1, pp. 151-216, Academic Press, London
10. Schutt, C. E. and Lindberg, U. (1992) Proc. Natl. Acad. Sci. U.SA 89, 319-323
11. Oosawa, F. (1980) Biophys. Chem. 11, 443-446
12. Erickson, H. P. (1989) J. Mol. Biol. 206, 465-474
13. Orlova, A. and Egelman, E. H. (1992) J. Mol. Biol. 227, 1043-1053
14. Orlova, A. and Egelman, E. H. (1993) J. Mol. Biol. 232, 334-341
15. Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F. and Holmes, K. C. (1990) Nature (London) 347, 37-44
16. McLaughlin, P. J., Gooch, J. T., Mannherz, H.-G. and Weeds, A. G. (1993) Nature (London) 364, 685-692
17. Schutt, C. E., Myslik, J. C., Rozycki, M. D., Goonesekere, N. C. W. and Lindberg, U. (1993) Nature (London) 365, 810-816
18. Tirion, M. M. and ben-Avraham, D. (1993) J. Mol. Biol. 230, 186-195
19. Isambert, H., Veniers, P., Maggs, A. C., Fattoum, A., Kassab, R., Pantaloni, D. and Carlier, M.-F. (1995) J. Biol. Chem. 270, 11437-11444
20. Carlier, M.-F. (1991) J. Biol. Chem. 266, 1-4
21. Estes, J. E., Selden, L. A., Kinosian, H. J. and Gershman, L. C. (1992) J. Muscle Res. Cell Motil. 13, 272-284
22. Orlova, A. and Egelman, E. H. (1995) J. Mol. Biol. 245, 582-597
23. Miki, M., Wahl, P. and Auchet, J.-C. (1982) Biophys. Chem. 16, 165-172
24. Miki, M. and Kouyama, T. (1994) Biochemistry 33, 10171-10177
25. S̄lósarek, G., Heintz, D. and Kalbitzer, H. R. (1994) FEBS Lett. 351, 405-410
26. Méjean, C., Hué, H. K., Pons, F., Roustan, C. and Benyamin, Y. (1988) Biochem. Biophys. Res. Commun. 152, 368-375
27. Adams, S. B. and Reisler, E. (1994) Biochemistry 33, 14426-14433
28. Strzelecka-Gołaszewska, H., Moraczewska, J., Khaitlina, S. Y. and Mossakowska, M. (1993) Eur. J. Biochem. 211, 731-742
29. Strzelecka-Gołaszewska, H., Woźniak, A. and Wawro, B. (1995) J. Muscle Res. Cell. Motil. 16, 152
30. Spudich, J. A. and Watt, S. (1971) J. Biol. Chem. 246, 4866-4871
31. Tawada, K., Wahl, P. and Auchet, J.-C. (1978) Eur. J. Biochem. 88, 411-419
32. Mossakowska, M., Moraczewska, J., Khaitlina, S. and Strzelecka-Gołaszewska, H. (1993) Biochem. J. 289, 897-902
33. Strzelecka-Gołaszewska, H., Mossakowska, M., Woźniak, A. and Nakayama, H. (1995) Biochem. J. 307, 527-534
34. Houk, W. T. and Ue, K. (1974) Anal. Biochem. 62, 66-74
35. Tao, T. and Cho, J. (1979) Biochemistry 18, 2759-2765
36. Laemmli, K. K. (1970) Nature (London) 227, 680-685
37. Matsudaira, P. (1987) J. Biol. Chem. 262, 10035-10038
38. Salinovich, O. and Montelaro, R. C. (1986) Anal. Biochem. 156, 341-347
39. Muhlrad, A., Cheung, P. C., Phan, B. C., Miller, C. and Reisler, E. (1994) J. Biol. Chem. 269, 11852-11858
40. Schwyter, D., Phillips, M. and Reisler, E. (1989) Biochemistry 28, 5889-5895
41. Mornet, D. and Ue, K. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 3680-3684
42. Elzinga, M., Collins, J. H., Kuehl, W. M. and Adelstein, R. S. (1973) Proc. Natl. Acad. Sci. U.S.A. 70, 2687-2691
43. Korn, E. D. (1982) Physiol. Rev. 62, 672-737
44. Selden, L. A., Gershman, L. C. and Estes, J. E. (1986) J. Muscle Res. Cell Motil. 7, 215-224
45. Kinosian, H. J., Selden, L. A., Estes, J. E. and Gershman, L. C. (1991) Biochim. Biophys. Acta 1077, 151-158
46. Jacobson, G. R. and Rosenbusch, J. P. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2742-2746
47. O'Donoghue, S. I., Miki, M. and dos Remedios, C. G. (1992) Arch. Biochem. Biophys. 293, 110-116
48. Frieden, C., Lieberman, D. and Gilbert, H. R. (1980) J. Biol. Chem. 255, 8991-8993
49. Frieden, C. and Patane, K. (1985) Biochemistry 24, 4192-4196
50. Drewes, G. and Faulstich, H. (1991) J. Biol. Chem. 266, 5508-5513
51. Lorenz, M., Popp, D. and Holmes, K. (1993) J. Mol. Biol. 234, 826-836
52. Tirion, M. M., ben-Avraham, D., Lorenz, M. and Holmes, K. C. (1995) Biophys. J. 68, 5-12
53. Selden, L. A., Estes, J. E. and Gershman, L. C. (1983) Biochem. Biophys. Res. Commun. 116, 478-485
54. Kim, E., Motoki, M., Seguro, K., Muhlrad, A. and Reisler, E. (1995) Biophys. J. 69, 2024-2032
55. Vahdat, A., Miller, C., Phillips, M., Muhlrad, A. and Reisler, E. (1995) FEBS Lett. 365, 149-151