Localization of Cys133 of rabbit skeletal troponin-I with respect to troponin-C by resonance energy transfer

Biophysical Journal

Volumn 74, Issue 6, 1998, Pages 3111-3119

  Luo, Yin ^a   Wu, Jing Lun ^a   Gergely, John ^a,b,c   Tao, Terence ^a,c,d  

^a BOSTON BIOMEDICAL RESEARCH INSTITUTE   (United States)

^b MASSACHUSETTS GENERAL HOSPITAL   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

^d TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MUSCLE PROTEIN; TROPONIN C; ADENOSINE TRIPHOSPHATASE; CYSTEINE; TROPONIN I;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; NONHUMAN; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; SKELETAL MUSCLE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; FLUORESCENCE POLARIZATION; KINETICS; METABOLISM; METHODOLOGY; MUSCLE FIBRIL; RABBIT; SPECTROFLUOROMETRY; TIME; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATASES; ANIMALS; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; FLUORESCENCE POLARIZATION; KINETICS; MODELS, MOLECULAR; MUSCLE, SKELETAL; MYOFIBRILS; PROTEIN CONFORMATION; RABBITS; SPECTROMETRY, FLUORESCENCE; TIME FACTORS; TROPONIN C; TROPONIN I;

EID: 0031595246     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)78017-8     Document Type: Article

References (42)

1. Botts, J., J. F. Thomason, and M. F. Morales. 1989. On the origin and transmission of force in actomyosin subfragment 1. Proc. Natl. Acad. Sci. USA. 86:2204-2208.
2. Chantler, P. D., T. Tao, and W. F. Stafford. 1991. On the relationship between distance information derived from cross-linking and from resonance energy transfer, with specific reference to sites located on myosin heads. Biophys. J. 59:1242-1250.
3. Dalbey, R. E., J. Weiel, and R. G. Yount. 1983. Forster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1. Biochemistry. 22:4696-4706.
4. Dale, R. E., and J. Eisinger. 1974. Intramolecular distances determined by energy transfer. Dependence on orientational freedom of donor and acceptor. Biopolymers. 13:1573-1605.
5. Dong, W.-J., M. Chandra, J. Xing, M. She, R. J. Solaro, and H. C. Cheung. 1997. Phosphorylation-induced distance change in a cardiac muscle troponin I mutant. Biochemistry. 36:6754-6761.
6. dos Remedios, C. G., and P. D. J. Moens. 1995. Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. J. Struct. Biol. 115:175-185.
7. Fairclough, R. H., and C. R. Cantor. 1978. The use of singlet-singlet transfer to study macromolecular assemblies. Methods Enzymol. 28: 347-379.
8. 2- and COOH-terminal regions of skeletal muscle troponin I. J. Biol. Chem. 269:5230-5240.
9. Farah, C. S., and F. C. Reinach. 1995. The troponin complex and regulation of muscle contraction. FASEB J. 9:755-767.
10. Fujimori, K., M. Sorenson, O. Herzberg, J. Moult, and F. C. Reinach. 1990. Probing the calcium-induced conformational transition of troponin-C with site-directed mutants. Nature. 345:182-184.
11. Gong, B.-J., Z. Wang, T. Tao, and J. Gergely. 1994. Troponin-C remains extended in the ternary troponin complex. Biophys. J. 66:A346.
12. Grabarek, Z., R.-Y. Tan, J. Wang, T. Tao, and J. Gergely. 1990. Inhibition of mutant troponin C activity by an intra-domain disulphide bond. Nature. 345:132-135.
13. Grabarek, Z., T. Tao, and J. Gergely. 1992. Molecular mechanism of troponin-C function. J. Muscle Res. Cell Motil. 13:383-393.
14. Greaser, M. L., and J. Gergely. 1973. Purification and properties of the components from troponin. J. Biol. Chem. 248:2125-2133.
15. Haas, E., M. Wilchek, E. Katchalsky-Katzir, and I. Z. Steinberg. 1975. Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer. Proc. Natl. Acad. Sci. USA. 72:1807-1811.
16. Herzberg, O., and M. N. G. James. 1985. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature. 313: 653-659.
17. Herzberg, O., and M. N. G. James. 1988. Refined crystal structure of troponin C from skeletal muscle at 2.0 Å resolution. J. Mol. Biol. 203:761-779.
18. 2+-induced conformational transition of troponin C. J. Biol. Chem. 261:2638-2644.
19. Ikura, M., G. M. Clore, A. M. Gronenborn, G. Zhu, C. B. Klee, and A. Bax, 1992. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science. 256:632-638.
20. Kekic, M., W. Huang, P. D. Moens, B. D. Hambly, and C. G. dos Remedios. 1996. Distance measurements near the myosin head-rod junction using fluorescence spectroscopy. Biophys. J. 71:40-47.
21. Kobayashi, T., T. Tao, J. Gergely, and J. H. Collins. 1994. Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants. J. Biol. Chem. 269:5725-5729.
22. 133 of troponin I in the ternary troponin complex and reconstituted thin filaments. Biochemistry. 36:11027-11035.
23. Meador, W. E., A. R. Means, and F. A. Quiocho. 1992. Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science. 257:1251-1255.
24. Miki, M., S. O'Donoghue, and C. dos Remedios. 1992. Structure of actin observed by fluorescence resonance energy transfer spectroscopy. J. Muscle Res. Cell Motil. 13:132-145.
25. 2+-bound complex: a small-angle x-ray and neutron scattering study. Biochemistry. 33:8233-8239.
26. 2+·troponin C complexed with troponin I by small-angle scattering. Biophys. J. 66: A311.
27. Park, H.-S., T. Tao, and P. D. Chantier. 1991. Proximity relationships between sites on myosin and actin. Biochemistry. 30:3189-3195.
28. Pearlstone, J. R., B. D. Sykes, and L. B. Smillie. 1997. Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I. Biochemistry. 36:7601-7606.
29. Perkins, W. J., J. Weiel, J. Grammer, and R. G. Yount. 1984. Introduction of a donor-acceptor pair by a single protein modification. J. Biol. Chem. 259:8786-8793.
30. Saijo, Y., S. Takeda, A. Scherer, T. Kobayashi, Y. Maeda, H. Taniguchi, M. Yao, and S. Wakatsuki. 1997. Production, crystallization, and preliminary x-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1-47) of troponin I. Protein Sci. 6:916-918.
31. Slupsky, C. M., and B. D. Sykes. 1995. NMR solution structure of calcium-saturated skeletal muscle troponin C. Biochemistry. 34: 15953-15964.
32. Small, E. W., and I. Isenberg. 1976. The use of moment index displacement in analyzing fluorescence time-decay data. Biopolymers. 15:1093-1100.
33. Stryer, L. 1978. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47:819-846.
34. Sundaralingam, M., R. Bergstrom, G. Strasburg, S. T. Rao, M. Greaser, and B. C. Wang. 1985. Molecular structure of troponin C from chicken skeletal muscle at 3 Å resolution. Science. 227:945-948.
35. Tao, T., and J. Cho. 1979. Fluorescence lifetime quenching studies on the accessibilities of actin sulfhydryl sites. Biochemistry. 18:2759-2765.
36. Tao, T., B.-J. Gong, and P. C. Leavis. 1990. Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments. Science. 247:1265-1372.
37. 2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex. Resonance energy transfer measurements. Biochemistry. 28:5902-5908.
38. Tao, T., M. L. Lamkin, and S. S. Lehrer. 1983. Excitation energy transfer studies of the proximity between tropomyosin and actin in reconstituted skeletal muscle thin filaments. Biochemistry. 22:3059-3066.
39. Tao, T., Y. Qian, I. Boldogh, and J. Gergely. 1995. Fluorescence lifetime, acrylamide quenching and photo-crosslinking studies of the interactions between troponin-I and troponin-T and monocysteine mutants of troponin-C. Biophys. J. 68:A166.
40. Wang, C.-K., and H. C. Cheung. 1986. Proximity relationship in the binary complex formed between troponin I and troponin C. J. Mol. Biol. 191:509-521.
41. 2+-triggered conformational transition in troponin C. Proc. Natl. Acad. Sci. USA. 89:11814-11817.
42. 2+-dependent interactions between the C-Helix of troponin-C and troponin-I. Photocrosslinking and fluorescence studies using a recombinant troponin-C. J. Biol. Chem. 265:4953-4957.