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Volumn 369, Issue 1, 2008, Pages 109-114

Spectroscopic and ITC study of the conformational change upon Ca2+-binding in TnC C-lobe and TnI peptide complex from Akazara scallop striated muscle

Author keywords

Ca2+; CD; ITC; NMR; TnC; TnI

Indexed keywords

CALCIUM ION; TROPONIN C; TROPONIN I;

EID: 40849147388     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.11.124     Document Type: Article
Times cited : (3)

References (39)
  • 1
    • 0000519978 scopus 로고
    • A new protein component participating in the superprecipitation of myosin B
    • Ebashi S., and Ebashi F. A new protein component participating in the superprecipitation of myosin B. J. Biochem. (Tokyo) 55 (1964) 604-613
    • (1964) J. Biochem. (Tokyo) , vol.55 , pp. 604-613
    • Ebashi, S.1    Ebashi, F.2
  • 2
    • 0013790350 scopus 로고
    • A new protein factor promoting aggregation of tropomyosin
    • Ebashi S., and Kodama A. A new protein factor promoting aggregation of tropomyosin. J. Biochem. (Tokyo) 58 (1965) 107-108
    • (1965) J. Biochem. (Tokyo) , vol.58 , pp. 107-108
    • Ebashi, S.1    Kodama, A.2
  • 3
    • 0023034376 scopus 로고
    • Regulatory and cytoskeletal proteins of vertebrate skeletal muscle
    • Ohtsuki I., Maruyama K., and Ebashi S. Regulatory and cytoskeletal proteins of vertebrate skeletal muscle. Adv. Protein Chem. 38 (1986) 1-68
    • (1986) Adv. Protein Chem. , vol.38 , pp. 1-68
    • Ohtsuki, I.1    Maruyama, K.2    Ebashi, S.3
  • 4
    • 0014128175 scopus 로고
    • A protein factor inhibiting the magnesium-activated adenosine triphosphatase of desensitized actomyosin
    • Hartshorne D.J., Perry S.V., and Schaub M.C. A protein factor inhibiting the magnesium-activated adenosine triphosphatase of desensitized actomyosin. Biochem. J. 104 (1967) 907-913
    • (1967) Biochem. J. , vol.104 , pp. 907-913
    • Hartshorne, D.J.1    Perry, S.V.2    Schaub, M.C.3
  • 6
    • 0015218120 scopus 로고
    • Reconstitution of troponin activity from three protein components
    • Greaser M.L., and Gergely J. Reconstitution of troponin activity from three protein components. J. Biol. Chem. 246 (1971) 4226-4233
    • (1971) J. Biol. Chem. , vol.246 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 7
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot A.S., and Potter J.D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Ann. Rev. Biophys. Chem. 16 (1987) 535-539
    • (1987) Ann. Rev. Biophys. Chem. , vol.16 , pp. 535-539
    • Zot, A.S.1    Potter, J.D.2
  • 8
    • 0015815403 scopus 로고
    • The amino acid sequence of rabbit skeletal muscle troponin C: gene replication and homology with calcium-binding proteins from carp and hake muscle
    • Collins J.H., Potter J.D., Horn M.J., Wilshire G., and Jackman N. The amino acid sequence of rabbit skeletal muscle troponin C: gene replication and homology with calcium-binding proteins from carp and hake muscle. FEBS Lett. 36 (1973) 268-272
    • (1973) FEBS Lett. , vol.36 , pp. 268-272
    • Collins, J.H.1    Potter, J.D.2    Horn, M.J.3    Wilshire, G.4    Jackman, N.5
  • 9
    • 0018873792 scopus 로고
    • Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene
    • Wilkinson J.M. Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene. Eur. J. Biochem. 103 (1980) 179-188
    • (1980) Eur. J. Biochem. , vol.103 , pp. 179-188
    • Wilkinson, J.M.1
  • 10
    • 0017233856 scopus 로고
    • Determination of the complete amino acid sequence of bovine cardiac troponin C
    • van Eerd J.P., and Takahashi K. Determination of the complete amino acid sequence of bovine cardiac troponin C. Biochemistry 15 (1976) 1171-1180
    • (1976) Biochemistry , vol.15 , pp. 1171-1180
    • van Eerd, J.P.1    Takahashi, K.2
  • 11
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter J.D., and Gergely J. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250 (1975) 4628-4633
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 13
    • 0039799573 scopus 로고    scopus 로고
    • Regulation of contraction by calcium binding myosins
    • Szent-Györgyi A.G. Regulation of contraction by calcium binding myosins. Biophys. Chem. 59 (1996) 357-363
    • (1996) Biophys. Chem. , vol.59 , pp. 357-363
    • Szent-Györgyi, A.G.1
  • 14
    • 0006975355 scopus 로고
    • The stoichiometry and location of troponin I- and troponin C-like proteins in the myofibril of the bay scallop, Aequipecten irradians
    • Lehman W., Head J.F., and Grant P.W. The stoichiometry and location of troponin I- and troponin C-like proteins in the myofibril of the bay scallop, Aequipecten irradians. Biochem. J. 171 (1980) 413-418
    • (1980) Biochem. J. , vol.171 , pp. 413-418
    • Lehman, W.1    Head, J.F.2    Grant, P.W.3
  • 15
    • 0022870153 scopus 로고
    • Troponin from Akazara scallop striated adductor muscles
    • Ojima T., and Nishita K. Troponin from Akazara scallop striated adductor muscles. J. Biol. Chem. 261 (1986) 16749-16754
    • (1986) J. Biol. Chem. , vol.261 , pp. 16749-16754
    • Ojima, T.1    Nishita, K.2
  • 16
    • 0027934639 scopus 로고
    • Amino acid sequence of troponin C from scallop striated adductor muscle
    • Nishita K., Tanaka H., and Ojima T. Amino acid sequence of troponin C from scallop striated adductor muscle. J. Biol. Chem. 269 (1994) 3464-3468
    • (1994) J. Biol. Chem. , vol.269 , pp. 3464-3468
    • Nishita, K.1    Tanaka, H.2    Ojima, T.3
  • 17
    • 0000183989 scopus 로고    scopus 로고
    • Bacterial expression, purification, and characterization of Akazara scallop troponin C
    • Ojima T., Maita T., Inoue A., and Nishita K. Bacterial expression, purification, and characterization of Akazara scallop troponin C. Fish. Sci. 63 (1997) 137-141
    • (1997) Fish. Sci. , vol.63 , pp. 137-141
    • Ojima, T.1    Maita, T.2    Inoue, A.3    Nishita, K.4
  • 18
    • 24644523695 scopus 로고    scopus 로고
    • Comparative studies on the functional roles of N- and C-terminal regions of molluskan and vertebrate troponin-I
    • Tanaka H., Takeya Y., Doi T., Yumoto F., Tanokura M., Ohtsuki I., Nishita K., and Ojima T. Comparative studies on the functional roles of N- and C-terminal regions of molluskan and vertebrate troponin-I. FEBS J. 17 (2005) 4475-4486
    • (2005) FEBS J. , vol.17 , pp. 4475-4486
    • Tanaka, H.1    Takeya, Y.2    Doi, T.3    Yumoto, F.4    Tanokura, M.5    Ohtsuki, I.6    Nishita, K.7    Ojima, T.8
  • 20
    • 0031707032 scopus 로고    scopus 로고
    • Amino acid sequence of troponin-I from Akazara scallop striated adductor muscle
    • Tanaka H., Ojima T., and Nishita K. Amino acid sequence of troponin-I from Akazara scallop striated adductor muscle. J. Biochem. 124 (1998) 304-310
    • (1998) J. Biochem. , vol.124 , pp. 304-310
    • Tanaka, H.1    Ojima, T.2    Nishita, K.3
  • 21
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg O., and James M.N.G. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature 313 (1985) 653-659
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 23
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagné S.M., Tsuda S., Li M.X., Smillie L.B., and Sykes B.D. Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nat. Struct. Biol. 9 (1995) 784-789
    • (1995) Nat. Struct. Biol. , vol.9 , pp. 784-789
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 24
    • 0032574791 scopus 로고    scopus 로고
    • Crystal structure of troponin C in complex with troponin I fragment at 2.3 Å resolution
    • Vassylyev D.G., Takeda S., Wakatsuki S., Maeda K., and Maéda Y. Crystal structure of troponin C in complex with troponin I fragment at 2.3 Å resolution. Proc. Natl. Acad. Sci. USA 95 (1998) 4847-4852
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4847-4852
    • Vassylyev, D.G.1    Takeda, S.2    Wakatsuki, S.3    Maeda, K.4    Maéda, Y.5
  • 32
    • 34447263324 scopus 로고    scopus 로고
    • The structure of Lethocerus troponin C: insights into the mechanism of stretch activation in muscles
    • De Nicola G., Burkart C., Qiu F., Agianian B., Labeit S., Martin S., Bullard B., and Pastore A. The structure of Lethocerus troponin C: insights into the mechanism of stretch activation in muscles. Structure 7 (2007) 813-824
    • (2007) Structure , vol.7 , pp. 813-824
    • De Nicola, G.1    Burkart, C.2    Qiu, F.3    Agianian, B.4    Labeit, S.5    Martin, S.6    Bullard, B.7    Pastore, A.8
  • 33
    • 0021267421 scopus 로고
    • Heat capacity and entropy changes of calmodulin induced by calcium binding
    • Tanokura M., and Yamada K. Heat capacity and entropy changes of calmodulin induced by calcium binding. J. Biochem. 95 (1984) 643-649
    • (1984) J. Biochem. , vol.95 , pp. 643-649
    • Tanokura, M.1    Yamada, K.2
  • 34
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai M., Huang Y., Sakaguchi K., Clore G.M., Gronenborn A.M., and Craigie R. An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11 (1998) 97-102
    • (1998) J. Biomol. NMR , vol.11 , pp. 97-102
    • Cai, M.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 36
    • 0026546294 scopus 로고
    • Conformational changes in the metal-binding sites of cardiac troponin C induced by calcium binding
    • Krudy G.A., Brito R.M., Putkey J.A., and Rosevear P.R. Conformational changes in the metal-binding sites of cardiac troponin C induced by calcium binding. Biochemistry 31 (1992) 1595-1602
    • (1992) Biochemistry , vol.31 , pp. 1595-1602
    • Krudy, G.A.1    Brito, R.M.2    Putkey, J.A.3    Rosevear, P.R.4
  • 37
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka N.C., and James M.N. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58 (1989) 951-998
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 38
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger R.H., and Nockolds C.E. Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem. 248 (1973) 3313-3326
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2


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