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Volumn 47, Issue 50, 2008, Pages 13383-13393

Structural studies of interactions between cardiac troponin I and actin in regulated thin filament using förster resonance energy transfer

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHEMICAL REACTIONS; ENERGY TRANSFER; FILAMENTS (LAMP); FLOW INTERACTIONS; IMAGE SEGMENTATION; LAWS AND LEGISLATION; MUSCLE; PHOSPHORYLATION; RESONANCE; SHRINKAGE; STRUCTURAL DYNAMICS;

EID: 57649123142     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801492x     Document Type: Article
Times cited : (19)

References (49)
  • 1
    • 0014609045 scopus 로고
    • Control of muscle contraction
    • Ebashi, S., Endo, M., and Otsuki, I. (1969) Control of muscle contraction. Q. Rev. Biophys. 2, 351-384.
    • (1969) Q. Rev. Biophys , vol.2 , pp. 351-384
    • Ebashi, S.1    Endo, M.2    Otsuki, I.3
  • 2
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C. S., and Reinach, F. C. (1995) The troponin complex and regulation of muscle contraction. FASEB J. 9, 755-767.
    • (1995) FASEB J , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 3
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., Homsher, E., and Regnier, M. (2000) Regulation of contraction in striated muscle. Physiol. Rev. 80, 853-924.
    • (2000) Physiol. Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 5
  • 6
    • 57649133043 scopus 로고    scopus 로고
    • Solaro, R. J. (2002) Modulation of cardiac myofilament activity by protein phosphorylation, in Handbook of Physiology. Section 2: The Cardiovascular System. I: The Heart (Page, E. F., Harry, A., and Solaro, R. J., Eds.) pp 264-300, Oxford University Press, Oxford.
    • Solaro, R. J. (2002) Modulation of cardiac myofilament activity by protein phosphorylation, in Handbook of Physiology. Section 2: The Cardiovascular System. Volume I: The Heart (Page, E. F., Harry, A., and Solaro, R. J., Eds.) pp 264-300, Oxford University Press, Oxford.
  • 7
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman, L. S. (1996) Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58, 447-481.
    • (1996) Annu. Rev. Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 9
    • 0030941244 scopus 로고    scopus 로고
    • Conformation of the N-terminal segment of a monocysteine mutant of troponin I from cardiac muscle
    • Dong, W. J., Chandra, M., Xing, J., Solaro, R. J., and Cheung, H. C. (1997) Conformation of the N-terminal segment of a monocysteine mutant of troponin I from cardiac muscle. Biochemistry 36, 6745-6753.
    • (1997) Biochemistry , vol.36 , pp. 6745-6753
    • Dong, W.J.1    Chandra, M.2    Xing, J.3    Solaro, R.J.4    Cheung, H.C.5
  • 10
    • 0035900569 scopus 로고    scopus 로고
    • 2+ induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin
    • 2+ induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin. J. Mol. Biol. 314, 51-61.
    • (2001) J. Mol. Biol , vol.314 , pp. 51-61
    • Dong, W.J.1    Xing, J.2    Robinson, J.M.3    Cheung, H.C.4
  • 11
    • 0020023850 scopus 로고
    • Preperation and identification of a- and b-Tropomyosins
    • Smillie, L. B. (1982) Preperation and identification of a- and b-Tropomyosins. Methods Enzymol. 85, 234-241.
    • (1982) Methods Enzymol , vol.85 , pp. 234-241
    • Smillie, L.B.1
  • 12
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and Spudich, J. A. (1982) Purification of muscle actin. Methods Enzymol. 85, 164-181.
    • (1982) Methods Enzymol , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 13
    • 0027931288 scopus 로고
    • Vanadate-induced changes in myosin subfragment-1 from cardiac muscle
    • Xing, J., and Cheung, H. C. (1994) Vanadate-induced changes in myosin subfragment-1 from cardiac muscle. Arch. Biochem. Biophys. 313, 229-234.
    • (1994) Arch. Biochem. Biophys , vol.313 , pp. 229-234
    • Xing, J.1    Cheung, H.C.2
  • 14
    • 0035909219 scopus 로고    scopus 로고
    • 2+-dependent, myosin subfragment 1-induced proximity changes between actin and the inhibitory region of troponin I
    • 2+-dependent, myosin subfragment 1-induced proximity changes between actin and the inhibitory region of troponin I. Biochim. Biophys. Acta 1549, 148-154.
    • (2001) Biochim. Biophys. Acta , vol.1549 , pp. 148-154
    • Kobayashi, T.1    Kobayashi, M.2    Collins, J.H.3
  • 15
    • 0025356099 scopus 로고
    • Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments
    • Tao, T., Gong, B. J., and Leavis, P. C. (1990) Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments. Science 247, 1339-1341.
    • (1990) Science , vol.247 , pp. 1339-1341
    • Tao, T.1    Gong, B.J.2    Leavis, P.C.3
  • 16
    • 2942607388 scopus 로고    scopus 로고
    • Switching of troponin I: Ca(2+) and myosin-induced activation of heart muscle
    • Robinson, J. M., Dong, W. J., Xing, J., and Cheung, H. C. (2004) Switching of troponin I: Ca(2+) and myosin-induced activation of heart muscle. J. Mol. Biol. 340, 295-305.
    • (2004) J. Mol. Biol , vol.340 , pp. 295-305
    • Robinson, J.M.1    Dong, W.J.2    Xing, J.3    Cheung, H.C.4
  • 18
    • 0034559235 scopus 로고    scopus 로고
    • Structural mapping of single cysteine mutants of cardiac troponin I
    • Dong, W. J., Xing, J., Chandra, M., Solaro, J., and Cheung, H. C. (2000) Structural mapping of single cysteine mutants of cardiac troponin I. Proteins 41, 438-447.
    • (2000) Proteins , vol.41 , pp. 438-447
    • Dong, W.J.1    Xing, J.2    Chandra, M.3    Solaro, J.4    Cheung, H.C.5
  • 19
    • 0023042747 scopus 로고
    • Proximity relationship in the binary complex formed between troponin I and troponin C
    • Wang, C. K., and Cheung, H. C. (1986) Proximity relationship in the binary complex formed between troponin I and troponin C. J. Mol. Biol. 191, 509-521.
    • (1986) J. Mol. Biol , vol.191 , pp. 509-521
    • Wang, C.K.1    Cheung, H.C.2
  • 20
    • 0030749604 scopus 로고    scopus 로고
    • Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C
    • She, M., Dong, W. J., Umeda, P. K., and Cheung, H. C. (1997) Time-resolved fluorescence study of the single tryptophans of engineered skeletal muscle troponin C. Biophys. J. 73, 1042-1055.
    • (1997) Biophys. J , vol.73 , pp. 1042-1055
    • She, M.1    Dong, W.J.2    Umeda, P.K.3    Cheung, H.C.4
  • 21
    • 0032555762 scopus 로고    scopus 로고
    • Calcium binding to the regulatory domain of skeletal muscle troponin C induces a highly constrained open conformation
    • She, M., Xing, J., Dong, W. J., Umeda, P. K., and Cheung, H. C. (1998) Calcium binding to the regulatory domain of skeletal muscle troponin C induces a highly constrained open conformation. J. Mol. Biol. 281, 445-452.
    • (1998) J. Mol. Biol , vol.281 , pp. 445-452
    • She, M.1    Xing, J.2    Dong, W.J.3    Umeda, P.K.4    Cheung, H.C.5
  • 22
    • 0024274005 scopus 로고
    • Distance distributions in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C
    • Lakowicz, J. R., Gryczynski, I., Cheung, H. C., Wang, C. K., Johnson, M. L., and Joshi, N. (1988) Distance distributions in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C. Biochemistry 27, 9149-9160.
    • (1988) Biochemistry , vol.27 , pp. 9149-9160
    • Lakowicz, J.R.1    Gryczynski, I.2    Cheung, H.C.3    Wang, C.K.4    Johnson, M.L.5    Joshi, N.6
  • 23
    • 0036409388 scopus 로고    scopus 로고
    • Activation of striated muscle: Nearest-neighbor regulatory-unit and cross-bridge influence on myofilament kinetics
    • Robinson, J. M., Wang, Y., Kerrick, W. G., Kawai, R., and Cheung, H. C. (2002) Activation of striated muscle: nearest-neighbor regulatory-unit and cross-bridge influence on myofilament kinetics. J. Mol. Biol. 322, 1065-1088.
    • (2002) J. Mol. Biol , vol.322 , pp. 1065-1088
    • Robinson, J.M.1    Wang, Y.2    Kerrick, W.G.3    Kawai, R.4    Cheung, H.C.5
  • 26
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • Takeda, S., Yamashita, A., Maeda, K., and Maeda, Y. (2003) Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 424, 35-41.
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 28
    • 44349116066 scopus 로고    scopus 로고
    • Structural basis for the regulation of muscle contraction by troponin and tropomyosin
    • Galinska-Rakoczy, A., Engel, P., Xu, C., Jung, H., Craig, R., Tobacman, L. S., and Lehman, W. (2008) Structural basis for the regulation of muscle contraction by troponin and tropomyosin. J. Mol. Biol. 379, 929-935.
    • (2008) J. Mol. Biol , vol.379 , pp. 929-935
    • Galinska-Rakoczy, A.1    Engel, P.2    Xu, C.3    Jung, H.4    Craig, R.5    Tobacman, L.S.6    Lehman, W.7
  • 29
    • 0038399765 scopus 로고    scopus 로고
    • Can Forster resonance energy transfer measurements uniquely position troponin residues on the actin filament? A case study in multiple-acceptor FRET
    • Robinson, J. M., Dong, W. J., and Cheung, H. C. (2003) Can Forster resonance energy transfer measurements uniquely position troponin residues on the actin filament? A case study in multiple-acceptor FRET. J. Mol. Biol. 329, 371-380.
    • (2003) J. Mol. Biol , vol.329 , pp. 371-380
    • Robinson, J.M.1    Dong, W.J.2    Cheung, H.C.3
  • 31
    • 0025572631 scopus 로고
    • The low-affinity Ca(2+)-binding sites in cardiac/slow skeletal muscle troponin C perform distinct functions: Site I alone cannot trigger contraction
    • Sweeney, H. L., Brito, R. M., Rosevear, P. R., and Putkey, J. A. (1990) The low-affinity Ca(2+)-binding sites in cardiac/slow skeletal muscle troponin C perform distinct functions: site I alone cannot trigger contraction. Proc. Natl. Acad. Sci. U.S.A. 87, 9538-9542.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 9538-9542
    • Sweeney, H.L.1    Brito, R.M.2    Rosevear, P.R.3    Putkey, J.A.4
  • 32
    • 0030904641 scopus 로고    scopus 로고
    • Phosphorylation-induced distance change in a cardiac muscle troponin I mutant
    • Dong, W. J., Chandra, M., Xing, J., She, M., Solaro, R. J., and Cheung, H. C. (1997) Phosphorylation-induced distance change in a cardiac muscle troponin I mutant. Biochemistry 36, 6754-6761.
    • (1997) Biochemistry , vol.36 , pp. 6754-6761
    • Dong, W.J.1    Chandra, M.2    Xing, J.3    She, M.4    Solaro, R.J.5    Cheung, H.C.6
  • 33
    • 40849150698 scopus 로고    scopus 로고
    • Structural changes of the regulatory proteins bound to the thin filaments in skeletal muscle contraction by X-ray fiber diffraction
    • Sugimoto, Y., Takezawa, Y., Matsuo, T., Ueno, Y., Minakata, S., Tanaka, H. and Wakabayashi, K. (2008) Structural changes of the regulatory proteins bound to the thin filaments in skeletal muscle contraction by X-ray fiber diffraction. Biochem. Biophys. Res. Commun. 369, 100-108.
    • (2008) Biochem. Biophys. Res. Commun , vol.369 , pp. 100-108
    • Sugimoto, Y.1    Takezawa, Y.2    Matsuo, T.3    Ueno, Y.4    Minakata, S.5    Tanaka, H.6    Wakabayashi, K.7
  • 34
    • 0037424545 scopus 로고    scopus 로고
    • 2+-induced conformational transition in the inhibitory and regulatory regions of cardiac troponin I
    • 2+-induced conformational transition in the inhibitory and regulatory regions of cardiac troponin I. J. Biol. Chem. 278. 8686-8692.
    • (2003) J. Biol. Chem , vol.278 , pp. 8686-8692
    • Dong, W.J.1    Robinson, J.M.2    Stagg, S.3    Xing, J.4    Cheung, H.C.5
  • 35
    • 15544390385 scopus 로고    scopus 로고
    • Calcium, thin filaments, and the integrative biology of cardiac contractility
    • Kobayashi, T., and Solaro, R. J. (2005) Calcium, thin filaments, and the integrative biology of cardiac contractility. Annu. Rev. Physiol. 67, 39-67.
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 39-67
    • Kobayashi, T.1    Solaro, R.J.2
  • 36
    • 17744382824 scopus 로고    scopus 로고
    • Structural based insights into the role of troponin in cardiac muscle pathophysiology
    • Li, M. X., Wang, X., and Sykes, B. D. (2004) Structural based insights into the role of troponin in cardiac muscle pathophysiology. J. Muscle Res. Cell Motil. 25, 559-579.
    • (2004) J. Muscle Res. Cell Motil , vol.25 , pp. 559-579
    • Li, M.X.1    Wang, X.2    Sykes, B.D.3
  • 37
    • 0033579814 scopus 로고    scopus 로고
    • Cooperativity and switching within the three-state model of muscle regulation
    • Maytum, R,, Lehrer, S. S., and Geeves, M. A. (1999) Cooperativity and switching within the three-state model of muscle regulation. Biochemistry 38, 1102-1110.
    • (1999) Biochemistry , vol.38 , pp. 1102-1110
    • Maytum, R.1    Lehrer, S.S.2    Geeves, M.A.3
  • 38
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop, D. F., and Geeves, M. A. (1993) Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65, 693-701.
    • (1993) Biophys. J , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 39
    • 4143107890 scopus 로고    scopus 로고
    • Kinetics of the structural transition of muscle thin filaments observed by fluorescence resonance energy transfer
    • Shitaka, Y., Kimura, C., Iio, T., and Miki, M. (2004) Kinetics of the structural transition of muscle thin filaments observed by fluorescence resonance energy transfer. Biochemistry 43, 10739-10747.
    • (2004) Biochemistry , vol.43 , pp. 10739-10747
    • Shitaka, Y.1    Kimura, C.2    Iio, T.3    Miki, M.4
  • 40
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel, R. D., and Weber, A. (1972) Cooperation within actin filament in vertebrate skeletal muscle. Nat. New Biol. 238, 97-101.
    • (1972) Nat. New Biol , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 41
    • 33644863664 scopus 로고    scopus 로고
    • Maximal activation of skeletal muscle thin filaments requires both rigor myosin S1 and calcium
    • Heeley, D. H., Belknap, B., and White, H. D. (2006) Maximal activation of skeletal muscle thin filaments requires both rigor myosin S1 and calcium. J. Biol. Chem. 281, 668-676.
    • (2006) J. Biol. Chem , vol.281 , pp. 668-676
    • Heeley, D.H.1    Belknap, B.2    White, H.D.3
  • 42
    • 0033862577 scopus 로고    scopus 로고
    • A model of troponin-I in complex with troponin-C using hybrid experimental data: The inhibitory region is a beta-hairpin
    • Tung, C. S., Wall, M. E., Gallagher, S. C., and Trewhella, J. (2000) A model of troponin-I in complex with troponin-C using hybrid experimental data: the inhibitory region is a beta-hairpin. Protein Sci. 9, 1312-1326.
    • (2000) Protein Sci , vol.9 , pp. 1312-1326
    • Tung, C.S.1    Wall, M.E.2    Gallagher, S.C.3    Trewhella, J.4
  • 43
    • 0030952840 scopus 로고    scopus 로고
    • Structural and functional domains of the troponin complex revealed by limited digestion
    • Takeda, S., Kobayashi, T., Taniguchi, H., Hayashi, H., and Maeda, Y. (1997) Structural and functional domains of the troponin complex revealed by limited digestion. Eur. J. Biochem. 246, 611-617.
    • (1997) Eur. J. Biochem , vol.246 , pp. 611-617
    • Takeda, S.1    Kobayashi, T.2    Taniguchi, H.3    Hayashi, H.4    Maeda, Y.5
  • 45
    • 0001224810 scopus 로고    scopus 로고
    • Modulation of cardiac troponin C-cardiac troponin I regulatory interactions by the amino-terminus of cardiac troponin I
    • Abbott, M. B., Dong, W. J., Dvoretsky, A., DaGue, B., Caprioli, R. M., Cheung, H. C., and Rosevear, P. R. (2001) Modulation of cardiac troponin C-cardiac troponin I regulatory interactions by the amino-terminus of cardiac troponin I. Biochemistry 40, 5992-6001.
    • (2001) Biochemistry , vol.40 , pp. 5992-6001
    • Abbott, M.B.1    Dong, W.J.2    Dvoretsky, A.3    DaGue, B.4    Caprioli, R.M.5    Cheung, H.C.6    Rosevear, P.R.7
  • 46
    • 0033546180 scopus 로고    scopus 로고
    • Gaponenko, V., Abusamhadneh, E., Abbott, M. B., Finley, N., Gasmi-Seabrook, G., Solaro, R. J., Rance, M., and Rosevear, P. R. (1999) Effects of troponin I phosphorylation on conformational exchange in the regulatory domain of cardiac troponin C. J. Biol. Chem. 274, 16681-16684.
    • Gaponenko, V., Abusamhadneh, E., Abbott, M. B., Finley, N., Gasmi-Seabrook, G., Solaro, R. J., Rance, M., and Rosevear, P. R. (1999) Effects of troponin I phosphorylation on conformational exchange in the regulatory domain of cardiac troponin C. J. Biol. Chem. 274, 16681-16684.
  • 47
    • 0027986739 scopus 로고
    • Coupling of calcium to the interaction of troponin I with troponin C from cardiac muscle
    • Liao, R., Wang, C. K., and Cheung, H. C. (1994) Coupling of calcium to the interaction of troponin I with troponin C from cardiac muscle. Biochemistry 33, 12729-12734.
    • (1994) Biochemistry , vol.33 , pp. 12729-12734
    • Liao, R.1    Wang, C.K.2    Cheung, H.C.3
  • 48
    • 0038001419 scopus 로고    scopus 로고
    • Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation
    • Heller, W. T., Finley, N. L., Dong, W. J., Timmins, P., Cheung, H. C., Rosevear, P. R., and Trewhella, J. (2003) Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation. Biochemistry 42, 7790-7800.
    • (2003) Biochemistry , vol.42 , pp. 7790-7800
    • Heller, W.T.1    Finley, N.L.2    Dong, W.J.3    Timmins, P.4    Cheung, H.C.5    Rosevear, P.R.6    Trewhella, J.7
  • 49
    • 34748818674 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin
    • Howarth, J. W., Meller, J., Solaro, R. J., Trewhella, J., and Rosevear, P. R. (2007) Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin. J. Mol. Biol. 373, 706-722.
    • (2007) J. Mol. Biol , vol.373 , pp. 706-722
    • Howarth, J.W.1    Meller, J.2    Solaro, R.J.3    Trewhella, J.4    Rosevear, P.R.5


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