Ca2+-induced conformational shift of the COOH-domain of eel skeletal muscle troponin C in the presence of physiological concentrations of Mg2+

Journal of Muscle Research and Cell Motility

Volumn 18, Issue 3, 1997, Pages 323-334

  François, Jean Marie ^a   Sedarous, Salah S ^b   Gerday, Charles ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b MAYO GRADUATE SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; MAGNESIUM ION; TROPONIN C;

ANIMAL CELL; ARTICLE; BINDING SITE; EEL; FLUORESCENCE; MUSCLE CONTRACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; SKELETAL MUSCLE; SPECTROSCOPY;

ACRYLAMIDE; ACRYLAMIDES; ANGUILLA; ANIMALS; CALCIUM; CESIUM; FLUORESCENCE POLARIZATION; IODINE; MAGNESIUM; MUSCLE, SKELETAL; NIACINAMIDE; OXYGEN; SPECTROPHOTOMETRY; STRUCTURE-ACTIVITY RELATIONSHIP; TROPONIN C;

EID: 0030915760     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018622109391     Document Type: Article

References (43)

1. ALCALA, J. R., GRATTON, E. & PRENDERGAST, F. G. (1987a) Resolvability of fluorescence lifetime distributions using phase fluorometry. Biophys. J. 51, 587-96.
2. ALCALA, J. R., GRATTON, E. & PRENDERGAST, F. G. (1987b) Fluorescence lifetime distributions in proteins. Biophys. J. 51, 597-604.
3. BAYLOR, S. M., CHANDLER, W. K. & MARSHALL, M. W. (1982) Optical measurements of intracellular pH and magnesium in frog skeletal muscle fibres. J. Physiol. 331, 105-37.
4. BRINLEY, F. J., SCARPA, A. & TIFFERT, T. (1977) The concentration of ionized magnesium in barnacle muscle fibers. J. Physiol. 266, 545-65.
5. 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C. Biochemistry 33, 2961-9.
6. CROW, M. T. & KUSHMERICK, M. J. (1982a) Myosin light chain phosphorylation is associated with a decrease in the energy cost for contraction in fast twitch mouse muscle. J. Biol. Chem. 257, 2121-4.
7. CROW, M. T. & KUSHMERICK, M. J. (1982b) Phosphorylation of myosin light chains in mouse fast-twitch muscle associated with reduced actomyosin turnover rate. Science 217, 835-7.
8. DECLERCQ, J.-P., TINANT, B., PARELLO, J. & RAMBAUD, J. (1991) Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments. J. Mol. Biol. 220, 1017-39.
9. FRANÇOIS, J.-M., SEDAROUS, S. S., GERDAY, C., GRATTON, E. & PRENDERGAST, F. G. (1987) Fluorescence lifetime distributions in eel troponin C and structurally homologous parvalbumins. Biophys. J. 51, 276a.
10. 2+ affinity constants of troponin C from eel skeletal muscle and positioning of the single tryptophan in the primary structure. J. Muscle Res. Cell Motil. 14, 585-93.
11. FRANÇOIS, J.-M., SHENG, Z., SZCZESNA, D. & POTTER, J. D. (1995) The functional role of the domains of troponin C investigated with thrombin fragments of troponin C reconstituted into skinned muscle fibers. J. Biol. Chem. 270, 19287-93.
12. GERDAY, C., FRANÇOIS, J.-M. & DUBOIS, I. (1984) Troponin C from eel (Anguilla anguilla) skeletal muscle: a protein containing one single tryptophan residue. Comparison with carp skeletal muscle troponin C. Mol. Physiol. 6, 43-54.
13. GILLIS, J.-M. (1985) Relaxation of vertebrate skeletal muscle. A synthesis of the biochemical and physiological approaches. Biochim. Biophys. Acta 811, 97-145.
14. GRATTON, E. & LIMKEMAN, M. (1983) A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution. Biophys. J. 44, 315-24.
15. 2+ in intact frog skeletal muscle. J. Biol. Chem. 255, 3987-92.
16. HERZBERG, O. & JAMES, M. N. G. (1985) Structure of the calcium regulatory muscle protein troponin C at 2.8 Å resolution. Nature 313, 653-9.
17. HESS, P., METZGER, P. & WEINGART, R. (1982) Free magnesium in sheep, ferret and frog striated muscle at rest measured with ion-selective micro-electrode. J. Physiol. 333, 173-88.
18. IO, T. & KONDO, H. (1981) Fluorescence titration and fluorescence stopped-flow studies on skeletal troponin C labeled with fluorescent maleimide reagent or dansylazyridine. J. Biochem. 90, 163-75.
19. 2+ exchange with troponin C. J. Biol. Chem. 254, 3497-502.
20. 2+-binding component of troponin. Biochem. Biophys. Res. Commun. 49, 898-5.
21. KRETSINGER, R. H. & NOCKOLDS, C. E. (1973) Carp muscle calcium-binding protein. J. Biol. Chem. 248, 3313-26.
22. LAKOWICZ, J. R. & WEBER, G. (1973) Quenching of protein fluorescence by oxygen. Detection of structural fluctuation in proteins on the nanosecond timescale. Biochemistry 12, 4171-9.
23. LEAVIS, P. C. & GERGELY, J. (1984) Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16, 235-305.
24. LEAVIS, P. C., NAGY, B., LEHRER, S. S., BIALKOWSKA, H. & GERGELY, J. (1980) Terbium binding to troponin C: binding stoichiometry and structural changes induced in the protein. Arch. Biochem. Biophys. 200, 17-21.
25. 1H-NMR study of the structure and interactions of the high affinity regions of troponin C. Biophys. J. 37, 35a.
26. LEVINE, B. A., THORNTON, J. M., FERNANDES, R., KELLY, C. M. & MERCOLA, D. (1978) Comparison of the calcium- and magnesium-induced structural changes of troponin C. A proton magnetic resonance study. Biochim. Biophys. Acta 535, 11-24.
27. MARTIN, R. B. & RICHARDSON, F. S. (1979) Lanthanides as probes for calcium in biological systems. Q. Rev. Biophys. 12, 181-209.
28. MARGOSSIAN, S. S. & STAFFORD, W. S. (1982) Calcium-induced dimerization of troponin-C J. Biol. Chem. 257, 1160-5.
29. 2+-binding proteins. Marker bands for identifying the types of coordination of the side-chain COO groups to metal ions in pike parvalbumin (pI = 4,10). FEBS Lett. 349, 84-8.
30. POTTER, J. D. & GERGELY, J. (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250, 4628-33.
31. 2+ and lanthanides. Biophys. J. 49, 107a.
32. 2+. Biophys. J. 34, 559-69.
33. SATYSHUR, K. A., RAO, S. T., PYZALSKA, D., DRENDEL, W., GREASER, M. & SUNDARALINGAM, M. (1988) Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-Å resolution. J. Biol. Chem. 263, 1628-47.
34. SHANNON, R. D. (1976) Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides. Acta Crystalog. A 32, 751-67.
35. STRICKLAND, E. H., HORWITZ, J., KAY, E., SHANNON, L. M., WILCHECK, M. & BILLUPS, L. (1971) Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearoyl-L-tryptophan M-hexyl ester. Biochemistry 10, 2631-8.
36. STULL, J. T., BLUMENTHAL, D. K. & COOKE, R. (1980) Regulation of contraction by myosin phosphorylation. A comparison between smooth and skeletal muscles. Biochem. Pharm. 29, 2537-43.
37. SUNDARALINGAM, M., BERGSTROM R., STRASBURG, G., RAO, S. T., ROYCHOWDHURY, P., GREASER, M. & WANG, B. C. (1985) Molecular structure of troponin C from chicken skeletal muscle at 3-Angstrom resolution. Science 227, 945-8.
38. TRIGO-GONZALEZ, G., RACHER, K., BURTNICK, L. & BORGFORD, T. (1992) A comparative spectroscopic study of tryptophan probes engineered into high- and low-affinity domains of recombinant chicken troponin C. Biochemistry 31, 7009-15.
39. TSALKOVA, T. N. & PRIVALOV, P. L. (1985) Thermodynamic study of domain organization in troponin C and calmodulin. J. Mol. Biol. 181, 533-44.
40. b excitation bands. Photochem. Photobiol. 25, 441-4.
41. WNUK, W. (1988) Calcium binding to troponin C and the regulation of muscle contraction: a comparative approach. In Calcium and Calcium Binding Proteins (edited by GERDAY. C., GILĹES, R. & BOLIS, L.), pp. 44-68. Berlin, Heidelberg: Springer-Verlag.
42. 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J. Biol. Chem. 257, 7678-83.
43. ZOT, A. S. & POTTER, J. D. (1987) Structural aspects of troponin-tropomyosin regulation, of skeletal muscle contraction. Ann. Rev. Biophys. Chem. 16, 535-59.