Structural interactions responsible for the assembly of the troponin complex on the muscle thin filament

Cell Structure and Function

Volumn 22, Issue 1, 1997, Pages 219-223

  Reinach, Fernando C ^a   Farah, Chuck S ^a   Monteiro, Patricia B ^a   Malnic, Bettina ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; TROPOMYOSIN; TROPONIN;

ACTIN FILAMENT; CONFERENCE PAPER; MUSCLE CONTRACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN PROTEIN INTERACTION; THIN FILAMENT;

EID: 0030994920     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.22.219     Document Type: Conference Paper

References (30)

1. ADELSTEIN, R.S. and EISENBERG, E. 1980. Regulation and kinetics of the action-myosin-ATP interaction. Ann. Rev. Biochem., 49: 921-956.
2. BREMEL, R.D. and WEBER, A. 1972. Cooperation within actin filament in vertebrate skeletal muscle. Nature, 238: 97-101.
3. CACHIA, P.J., EYK, J.V., INGRAHAM, P.H., MCCUBBIN, W.D., KAY, C.M., and HODGES, R.S. 1986. Calmodulin and troponin C: a comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]. Biochemistry, 25: 3553-3562.
4. CHACKO, S. and EISENBERG, E. 1990. Cooperativity of actin-activated ATPase of gizzard heavy meromyosin in the presence of gizzard tropomyosin. J. Biol. Chem., 265: 2105-2110.
5. CHO, Y.-J., LIU, J., and HITCHCOCK-DEGREGORI, S.E. 1990. The amino terminus of muscle tropomyosin is a major determinant for function. J. Biol. Chem., 265: 538-545.
6. DAHIYA, R., BUTTERS, C.A., and TOBACMAN, L.S. 1994. Equilibrium linkage analysis of cardiac thin filament assembly. Implications for the regulation of muscle contraction. J. Biol. Chem., 269: 29457-29461.
7. 2+, KC1, Troponin I, and troponin C. Biochemistry, 14: 2718-2725.
8. 2- and COOH-terminal regions of skeletal muscle troponin I. J. Biol. Chem., 269: 5230-5240.
9. FARAH, C.S. and REINACH, F.C. 1995. The troponin complex and regulation of muscle contraction. FASEB J., 9: 755-767.
10. 2+ sensitivity of thin filament assembly. J. Biol. Chem., 270: 25455-25460.
11. FLICKER, P.F., PHILLIPS JR, G.N., and COHEN, C. 1982. Troponin and its Interactions with Tropomyosin, an Electron Microscope Study. J. Mol. Biol., 162: 495-501.
12. GEEVES, M.A. and LEHRER, S.S. 1994. Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit. Biophys. J., 67: 273-282.
13. HAMMELL, R.L. and HITCHCOCK-DEGREGORI, S.E. 1996. Mapping the functional domains within the carboxyl terminus of α-tropomyosin encoded by the alternatively spliced ninth exon. J. Biol. Chem., 271: 4236-4242.
14. HEALD, R.W. and HITCHCOCK-DEGREGORI, S.E. 1988. The structure of the amino terminus of tropomyosin is critical for binding to action in the absence and presence of troponin. J. Biol. Chem., 263: 5254-5259.
15. HEELEY, D.H., WATSON, M.H., MAK, A.S., DUBORD, P., and SMILLIE, L.B. 1989. Effect of phosphorylation on the interaction and functional properites of rabbit striated muscle alfa /alfa tropomyosin. J. Biol. Chem., 264: 2424-2439.
16. HERZBERG, O. and JAMES, M.N.G. 1988. Refined crystal structure of troponin C from turkey skeletal myscle at 2.0 A resolution. J. Mol. Biol., 203: 761-779.
17. HILL, L.E., MEHEGAN, J.P., BUTTERS, C.A., and TOBACMAN, L.S. 1992. Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules. J. Biol. Chem., 267: 16106-16113.
18. HOLROYDE, M.J., ROBERTSON, S.R., JOHNSON, J.D., SOLARO, R.J., and POTTER, J.D. 1980. The calcium and magnesium binding sites on cardiac troponin their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem., 255: 11688-11693.
19. 2+ exchange with troponin C. J. Biol. Chem., 254: 3497-3502.
20. 2+-specific regulatory sites of troponin C. J. Biol. Chem., 269: 8919-8923.
21. MALNIC, B. and REINACH, F.C. 1994. Assembly of functional skeletal muscle troponin complex in E. coli. Eur. J. Biochem., 222(1): 49-54.
22. MONTEIRO, P.B., LATARO, R.C., FERRO, J.A., and REINACH, F.C. 1994. Functional alfa-tropomyosin produced in E. coli. A di-peptide extension can substitute the N-terminal acetyl group. J. Biol. Chem., 269: 10461-10466.
23. OHTSUKI, I. 1979. Molecular arrangement of troponin-T in the filament. J. Biochem., 86: 491-497.
24. 2+. Regulation of muscle contraction. Biochemistry, 13: 2697-2703.
25. POTTER, J.D. and GERGELY, J. 1975. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrilar ATPase. J. Biol. Chem., 250: 4628-4633.
26. SORENSON, M.M., DA SILVA, A.C.R., GOUVEIA, C.S., SOUSA, V.P., OSHIMA, W., FERRO, J.A., and REINACH, F.C. 1995. Concerted action of the high affinity calcium binding sites in skeletal muscle troponin C. J. Biol. Chem., 270: 9770-9777.
27. SYSKA, H., WILKINSON, J.M., GRAND, R.J.A., and PERRY, S.V. 1976. The relationship between biological activity primary structure of troponin I from white skeletal muscle of the rabbit. Biochem. J., 153: 375-387.
28. 2+ binding sites of troponin C in the regulation of skeletal muscle contraction. J. Biol. Chem., 271: 8381-8386.
29. TALBOT, J.A. and HODGES, R.S. 1981. Synthetic studies on the inhibitory region of rabbit skeletal troponin I. J. Biol. Chem., 256: 2798-2802.
30. TANOKURA, M., TAWADA, Y., ONO, A., OHTSUKI, I. 1983. Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interaction with tropomyosin, troponin I and troponin C. J. Biochem., 93: 331-337.