Caldesmon reduces the apparent rate of binding of myosin s1 to actin-tropomyosin

Biochemistry

Volumn 40, Issue 19, 2001, Pages 5757-5764

  Sen, Anindita ^a   Chen, Yi Der ^b   Yan, Bo ^b   Chalovich, Joseph M ^a  

^a EAST CAROLINA UNIVERSITY   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; LABORATORIES; MOLECULES;

BINDING;

PROTEINS;

ACTIN; CALDESMON; MYOSIN SUBFRAGMENT 1; TROPOMYOSIN;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; COMPLEX FORMATION; PRIORITY JOURNAL; PROTEIN BINDING;

ACTINS; ANIMALS; CALMODULIN-BINDING PROTEINS; FLUORESCEIN; FLUORESCEINS; FLUORESCENT DYES; IODOACETAMIDE; KINETICS; LIGHT; MYOSIN SUBFRAGMENTS; OXADIAZOLES; PROTEIN BINDING; PYRENES; RABBITS; SALICYLIC ACIDS; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE; TROPOMYOSIN; TURKEYS;

EID: 0035873925     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi002724t     Document Type: Article

References (46)

1. Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 5652-5655.
2. Brenner, B., Yu, L.C., and Chalovich, J. M. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 5739-5743.
3. Pfitzer, G., Zeugner, C., Troschka, M., and Chalovich, J. M. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 5904-5908.
4. Malmquist, U., Arner, A., Makuch, R., and Dabrowska, R. (1996) Pfluegers Arch. 432, 241-247.
5. Smith, C. W. J., Pritchard, K., and Marston, S. B. (1987) J. Biol. Chem. 262, 116-122.
6. Velaz, L., Hemric, M. E., Benson, C. E., and Chalovich, J. M. (1989) J. Biol. Chem. 264, 9602-9610.
7. Chalovich, J. M., Cornelius, P., and Benson, C. E. (1987) J. Biol. Chem. 262, 5711-5716.
8. Horiuchi, K. Y., and Chacko, S. (1989) Biochemistry 28, 9111-9116.
9. Chalovich, J. M., and Pfitzer, G. (1997) in Cellular Aspects of Smooth Muscle Function (Kao, C. Y., and Carsten, M. E., Eds.) pp 253-287, Cambridge University Press, Cambridge, U.K.
10. Chalovich, J. M., Sen, A., Resetar, A., Leinweber, B., Fredricksen, R. S., Lu, F., and Chen, Y.-D. (1998) Acta Physiol. Scand. 164, 427-435.
11. Marston, S. B., and Redwood, C. S. (1992) J. Biol. Chem. 267, 16796-16800.
12. Marston, S. B., and Redwood, C. S. (1993) J. Biol. Chem. 268, 12317-12320.
13. Hemric, M. E., and Chalovich, J. M. (1988) J. Biol. Chem. 263, 1878-1885.
14. Ikebe, M., and Reardon, S. (1998) J. Biol. Chem. 263, 3055-3058.
15. Chen, Y.-D., and Chalovich, J. M. (1992) Biophys. J. 63, 1063-1070.
16. Sen, A., and Chalovich, J. M. (1998) Biochemistry 37, 7526-7531.
17. Eisenberg, E., and Kielley, W. W. (1972) Cold Spring Harbor Symp. Quant. Biol. 37, 145-152.
18. Kielley, W. W., and Harrington, W. F. (1960) Biochim. Biophys. Acta 41, 401-421.
19. Weeds, A. G., and Taylor, R. S. (1975) Nature 275, 54-56.
20. Bretscher, A. (1984) J. Biol. Chem. 259, 12873-12880.
21. Graceffa, P., Jansco, A., and Mabuchi, K. (1992) Arch. Biochem. Biophys. 297, 46-51.
22. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275.
23. Laemmli, U. K. (1970) Nature 227, 680-685.
24. Brenner, S. L., and Korn, E. D. (1983) J. Biol. Chem. 258, 5013-5020.
25. Kouyama, T., and Mihashi, K. (1981) Eur. J. Biochem. 114, 33-38.
26. Lin, S.-H., and Cheung, H. C. (1991) Biochemistry 30, 4317-4322.
27. Lin, S.-H., Harzelrig, J. B., and Cheung, H. C. (1993) Biophys. J. 65, 1433-1444.
28. Trayer, H. R., and Trayer, I. P. (1988) Biochemistry 27, 5718-5727.
29. Aguirre, R., Gonsoulin, F., and Cheung, H. C. (1986) Biochemistry 25, 6827-6835.
30. McGhee, J. D., and vonHippel, P. H. (1974) J. Mol. Biol. 86, 469-489.
31. Hill, T. L., Eisenberg, E., and Greene. L. E. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 3186-3190.
32. Hill, T. L., Eisenberg, E., and Chalovich, J. M. (1981) Biophys. J. 35, 99-112.
33. Graceffa, P. (1999) Biochemistry 38, 11984-11992.
34. Sobieszek, A (1982) J. Mol. Biol. 157, 275-286.
35. Williams. D. L., Greene, L. E., and Eisenberg, E. (1984) Biochemistry 23, 4150-4155.
36. Lehrer, S. S., and Morris, E. P. (1984) J. Biol. Chem. 259, 2070-2072.
37. Chacko, S., and Eisenberg, E. (1990) J. Biol. Chem. 265, 2105-2110.
38. Trybus, K. M., and Taylor, E. W. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 7209-7213.
39. McKillop, D. F. A., and Geeves, M. A. (1993) Biophys. J. 65, 693-701.
40. McKillop, D. F. A., and Geeves, M. A. (1991) Biochem. J. 279, 711-718.
41. Chen, Y.-D., Yan, B., Chalovich, J. M., and Brenner, B. (2000) Biophys. J. 78, 236A.
42. Marston, S. B., Fraser, I. D. C., and Huber, P. A. J. (1994) J. Biol. Chem. 269, 32104-32109.
43. Marston, S. B. (1988) FEBS Lett. 238, 147-150.
44. Horiuchi, K. Y., Samuel, M., and Chacko, S. (1991) Biochemistry 30, 712-717.
45. Szczesna, D., Graceffa, P., Wang, C.-L. A., and Lehrer, S. S. (1994) Biochemistry 33, 6716-6720.
46. Fraser, I. D. C., Copeland, O., Bing, W., and Marston, S. B. (1997) Biochemistry 36, 5483-5492.