Bacterial Expression, Purification, and Characterization of Akazara Scallop Troponin C

Fisheries Science

Volumn 63, Issue 1, 1997, Pages 137-141

  Ojima, Takao ^a   Maita, Michiko ^a   Inoue, Akira ^a   Nishita, Kiyoyoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Bacterial expression; Ca2+ regulation; cDNA cloning; Scallop; Troponin C

Indexed keywords

BACTERIA (MICROORGANISMS); CHLAMYS NIPPONENSIS AKAZARA; ESCHERICHIA COLI;

EID: 0000183989     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.2331/fishsci.63.137     Document Type: Article

References (28)

1. S. Ebashi and F. Ebashi: A new protein component participating in the superprecipitation of myosin B. J. Biochem., 55, 604-613 (1964).
2. S. Ebashi and A. Kodama: A new protein factor promoting aggregation of tropomyosin. J. Biochem., 58, 107-108 (1965).
3. D. J. Hartshorne and H. Mueller: Separation and recombination of the ethylene glycol bis (β-aminoethylether)-N,N,N′,N′-tetraacetic acid-sensitizing factor obtained from a low ionic strength extract of natural actomyosin. J. Biol. Chem., 242, 3089-3092 (1967).
4. S. Ebashi, I. Ohtsuki, and K. Mihashi: Regulatory proteins of muscle with special reference to troponin. Cold Spring Harbor Symp. Quant. Biol., 37, 215-233 (1972).
5. I. Ohtsuki, K. Maruyama, and S. Ebashi: Regulatory and cytoskeletal proteins of vertebrate skeletal muscle. Adv. Prot. Chem., 38, 1-67 (1986).
6. O. Herzberg and M. N. James: Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature, 313, 653-659 (1985).
7. M. Sundaralingam, R. Bergstrom, G. Strasburg, S. T. Rao, P. Roychowdhury, M. Greaser, and B. C. Wang: Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution. Science, 227, 945-948 (1985).
8. J. H. Collins: Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons. J. Muscle Res. Cell Motil., 12, 3-25 (1991).
9. F. C. Reinach and R. Karlsson: Cloning, expression, and site-directed mutagenesis of chicken skeletal muscle troponin C. J. Biol. Chem., 263, 2371-2376 (1988).
10. Z. Dobrowolski, G. Q. Xu, W. Chen, and S. E. Hitchcock-DeGregori: Analysis of the regulatory and structural defects of troponin C central helix mutants. Biochemistry, 30, 7089-7096 (1991).
11. L. Smith, N. J. Greenfield, and S. E. Hitchcock-DeGregori: The effects of deletion of the amino-terminal helix on troponin C function and stability. J. Biol. Chem., 269, 9857-9863 (1994).
12. M. X. Li, S. M. Gagne, S. Tsuda, C. M. Kay, L. B. Smillie, and B. D. Sykes: Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner. Biochemistry, 34, 8330-8340 (1995).
13. T. Ojima and K. Nishita: Troponin from akazara scallop striated adductor muscles. J. Biol. Chem., 261, 16749-16754 (1986).
14. 2+-induced conformational change and interaction with rabbit troponin subunits. Arch. Biochem. Biophys., 299, 344-349 (1992).
15. K. Nishita, H. Tanaka, and T. Ojima: Amino acid sequence of troponin C from scallop striated adductor muscle. J. Biol. Chem., 269, 3464-3468 (1994).
16. T. Ojima, H. Tanaka, and K. Nishita: Cloning and sequence of a cDNA encoding akazara scallop troponin C. Arch. Biochem. Biophys., 311, 272-276 (1994).
17. F. W. Studier and B. A. Moffatt: Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol., 189, 113-130 (1986).
18. R. Steen, A. E. Dahlberg, B. N. Lade, F. W. Studier, and J. J. Dunn: T7 RNA polymerase directed expression of the Escherichia coli rrnB operon. EMBO J., 5, 1099-1103 (1986).
19. S. W. Lin, J. J. Dunn, F. W. Studier, and D. W. Stafford: Expression of human factor IX and its subfragments in Escherichia coli and generation of antibodies to the subfragments. Biochemistry, 26, 5267-5274 (1987).
20. F. W. Studier, A. H. Rosenberg, J. J. Dunn, and J. W. Dubendorff: Use of T7 RNA polymerase to direct expression of cloned genes, in "Methods in Enzymology" (ed. by J. N. Abelson) Vol. 185, Academic Press, New York, 1990, pp. 60-89.
21. T. Ojima and K. Nishita: Separation of akazara scallop and rabbit troponin components by a single step chromatography on CM-Toyopearl. J. Biochem., 104, 9-11 (1988).
22. T. Ojima and K. Nishita: Comparative studies on biochemical properties of troponins from ezo-giant scallop (Patinopecten yessoensis) and akazara scallop (Chlamys nipponensis akazara). Comp. Biochem. Physiol., 103B, 727-732 (1992).
23. H. Harafuji and Y. Ogawa: Re-examination of the apparent binding constant of ethylene glycol bis (β-aminoethylether)-N,N′-tetraacetic acid with calcium around neutral pH. J. Biochem., 87, 1305-1312 (1980).
24. S. V. Perry: Myosin adenosinetriphosphatase, in "Method in Enzymology" (ed. by S. P. Colowick and N. O. Kaplan.) Vol. 2, Academic Press, New York, 1955, pp. 582-588.
25. J. A. Spudich and S. Watt: The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragment of myosin. J. Biol. Chem., 246, 4866-4871 (1971).
26. M. A. Porzio and A. M. Pearson: Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim. Biophys. Acta, 490, 27-34 (1977).
27. A. G. Gornall, C. S. Bardawill, and M. N. David: Determination of serum proteins by means of the biuret reaction. J. Biol. Chem., 177, 751-766 (1949).
28. W. Liu, D. G. Dotson, X. Lin, J. J. Mullen, M. L. Gonzalez-Garay, Q. Lu, and J. A. Putkey: The presence but not the sequence of the N-terminal peptide in cardiac TnC is important for function. FEBS Letters, 347, 152-156 (1994).