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Volumn 246, Issue 3, 1997, Pages 611-617

Structural and functional domains of the troponin complex revealed by limited digestion

Author keywords

Calcium; Domain structure; Limited digestion; Muscle regulation; Troponin

Indexed keywords

ADENOSINE TRIPHOSPHATASE; TROPONIN;

EID: 0030952840     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00611.x     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 0014396206 scopus 로고
    • Calcium ion and muscle contraction
    • Ebashi, S. & Endo, M. (1968) Calcium ion and muscle contraction, Prog. Biophys. Mol. Biol. 18, 123-183.
    • (1968) Prog. Biophys. Mol. Biol. , vol.18 , pp. 123-183
    • Ebashi, S.1    Endo, M.2
  • 2
    • 0021151109 scopus 로고
    • Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction
    • Leavis, P. C. & Gergely, J. (1984) Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction, CRC Crit. Rev. Biochem. 16, 235-305.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 235-305
    • Leavis, P.C.1    Gergely, J.2
  • 3
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot, A. S. & Potter, J. D. (1987) Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction, Annu. Rev. Biophys. Biophys. Chem. 16, 535-559.
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 4
    • 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
  • 5
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg, O. & James, M. N. G. (1985) Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution, Nature 313, 653-659.
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 8
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C. S. & 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
  • 9
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky, C. M. & Sykes, B. D. (1995) NMR solution structure of calcium-saturated skeletal muscle troponin C, Biochemistry 34, 15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 12
    • 0028077249 scopus 로고
    • 2+-troponin C-troponin I derived from small-angle scattering data
    • 2+-troponin C-troponin I derived from small-angle scattering data. Biochemistry 33, 12800-12806.
    • (1994) Biochemistry , vol.33 , pp. 12800-12806
    • Olah, G.A.1    Trewhella, J.2
  • 13
    • 0019887810 scopus 로고
    • Study of the structure of troponin-T by measuring the relative reactivities of lysine with acetic anhydride
    • Hitchcock, S. E., Zimmerman, C. J. & Smalley, C. (1981) Study of the structure of troponin-T by measuring the relative reactivities of lysine with acetic anhydride, J. Mol. Biol. 147, 125-151.
    • (1981) J. Mol. Biol. , vol.147 , pp. 125-151
    • Hitchcock, S.E.1    Zimmerman, C.J.2    Smalley, C.3
  • 14
    • 0019887809 scopus 로고
    • Study of the structure of troponin-C by measuring the relative reactivities of lysine with acetic anhydride
    • Hitchcock, S. E. (1981) Study of the structure of troponin-C by measuring the relative reactivities of lysine with acetic anhydride, J. Mol. Biol. 147, 153-173.
    • (1981) J. Mol. Biol. , vol.147 , pp. 153-173
    • Hitchcock, S.E.1
  • 15
    • 0020479286 scopus 로고
    • Study of the structure of troponin-I by measuring the relative reactivities of lysine with acetic anhydride
    • Hitchcock-DeGregori, S. E. (1982) Study of the structure of troponin-I by measuring the relative reactivities of lysine with acetic anhydride, J. Biol. Chem. 257, 7372-7380.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7372-7380
    • Hitchcock-DeGregori, S.E.1
  • 16
    • 0019335170 scopus 로고
    • Direct evidence for the calcium-induced change in the quaternary structure of troponin in situ
    • Sutoh, K. (1980) Direct evidence for the calcium-induced change in the quaternary structure of troponin in situ, Biochemistry 19, 1977-1983.
    • (1980) Biochemistry , vol.19 , pp. 1977-1983
    • Sutoh, K.1
  • 17
    • 0025714052 scopus 로고
    • 2+-dependent interaction between the C-helix of tropnin C and troponin I
    • 2+-dependent interaction between the C-helix of tropnin C and troponin I, J. Biol. Chem. 265, 4953-4957.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4953-4957
    • Wang, Z.1    Sarker, S.2    Gergely, J.3    Tao, T.4
  • 19
    • 0029039847 scopus 로고
    • Calcium-induced troponin flexibility revealed by distance distribution measurements between engineered sites
    • Zhao, X., Kobayashi, T., Malak, H., Gryczynski, I., Lakowicz, J., Wade, R. & Collins, J. H. (1995) Calcium-induced troponin flexibility revealed by distance distribution measurements between engineered sites, J. Biol. Chem. 270, 15507-15514.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15507-15514
    • Zhao, X.1    Kobayashi, T.2    Malak, H.3    Gryczynski, I.4    Lakowicz, J.5    Wade, R.6    Collins, J.H.7
  • 20
    • 0021251356 scopus 로고
    • Troponin-tropomyosin interactions
    • Morris, E. P. & Lehrer, S. S. (1984) Troponin-tropomyosin interactions, Biochemistry 23, 2214-2220.
    • (1984) Biochemistry , vol.23 , pp. 2214-2220
    • Morris, E.P.1    Lehrer, S.S.2
  • 21
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana, A., Fassina, G., Vita, C., Dalzoppo, D., Zamai, M. & Zambonin, M. (1986) Correlation between sites of limited proteolysis and segmental mobility in thermolysin, Biochemistry 25, 1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 23
    • 0021845498 scopus 로고
    • Tropomyosin lysine reactivities and relationship to coiled-coil structure
    • Hitchcock-DeGregori, S. E., Lewis, S. F. & Chou, T. M.-T. (1985) Tropomyosin lysine reactivities and relationship to coiled-coil structure, Biochemists 24, 3305-3314.
    • (1985) Biochemists , vol.24 , pp. 3305-3314
    • Hitchcock-DeGregori, S.E.1    Lewis, S.F.2    Chou, T.M.-T.3
  • 24
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction
    • Spudich, J. A. & Watt, S. (1971) The regulation of rabbit skeletal muscle contraction, J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 25
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G. & Taylor, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin, Nature 257, 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 26
    • 0028819391 scopus 로고
    • Functional chicken gizzard heavy meromyosin expression in and purification from baculovirus-infected insect cells
    • Onishi, H., Maeda, K., Maéda, Y., Inoue, A. & Fujiwara, K. (1995) Functional chicken gizzard heavy meromyosin expression in and purification from baculovirus-infected insect cells, Proc. Natl Acad. Sci. USA 92, 704-708.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 704-708
    • Onishi, H.1    Maeda, K.2    Maéda, Y.3    Inoue, A.4    Fujiwara, K.5
  • 27
    • 0020490904 scopus 로고
    • Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
    • Lehrer, S. S. & Morris, E. P. (1982) Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase, J. Biol. Chem. 257, 8073-8080.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8073-8080
    • Lehrer, S.S.1    Morris, E.P.2
  • 28
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. & von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 29
    • 0028021757 scopus 로고
    • A mass spectrometric study on the in vivo posttranslational modification of GAP-43
    • Taniguchi, H., Suzuki, M., Manenti, S. & Titani, K. (1994) A mass spectrometric study on the in vivo posttranslational modification of GAP-43, J. Biol. Chem. 269, 22481-22484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22481-22484
    • Taniguchi, H.1    Suzuki, M.2    Manenti, S.3    Titani, K.4
  • 30
    • 0018695446 scopus 로고
    • Molecular arrangement of troponin-T in the thin filament
    • Ohtsuki, I. (1979) Molecular arrangement of troponin-T in the thin filament, J. Biochem. (Tokyo) 86, 491-497.
    • (1979) J. Biochem. (Tokyo) , vol.86 , pp. 491-497
    • Ohtsuki, I.1
  • 31
    • 0020122663 scopus 로고
    • Chymotryptic subfragments of troponin T from rabbit skeletal muscle
    • Tanokura, M., Tawada, Y. & Ohtsuki, I. (1982) Chymotryptic subfragments of troponin T from rabbit skeletal muscle, J. Biochem. (Tokyo) 91, 1257-1265.
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1257-1265
    • Tanokura, M.1    Tawada, Y.2    Ohtsuki, I.3
  • 33
    • 0016213363 scopus 로고
    • 2+ regulation of muscle contraction
    • 2+ regulation of muscle contraction, Biochemistry 13, 2697-2703.
    • (1974) Biochemistry , vol.13 , pp. 2697-2703
    • Potter, J.D.1    Gergely, J.2
  • 34
    • 0016610748 scopus 로고
    • Regulation of muscle contraction
    • Hitchcock, S. E. (1975) Regulation of muscle contraction, Eur. J. Biochem. 52, 255-263.
    • (1975) Eur. J. Biochem. , vol.52 , pp. 255-263
    • Hitchcock, S.E.1
  • 35
    • 0028864262 scopus 로고
    • Separation and characterization of the two functional regions of troponin involved in muscle thin filament regulation
    • Schaertl, S., Lehrer, S. S. & Geeves, M. A. (1995) Separation and characterization of the two functional regions of troponin involved in muscle thin filament regulation, Biochemistry 34, 15890-15894.
    • (1995) Biochemistry , vol.34 , pp. 15890-15894
    • Schaertl, S.1    Lehrer, S.S.2    Geeves, M.A.3
  • 37
    • 0025911961 scopus 로고
    • Crosslinking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I
    • Kobayashi, T., Tao, T., Grabarek, Z., Gergely, J. & Collins, J. H. (1991) Crosslinking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I, J. Biol. Chem. 266, 13746-13751.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13746-13751
    • Kobayashi, T.1    Tao, T.2    Grabarek, Z.3    Gergely, J.4    Collins, J.H.5
  • 38
    • 0023042747 scopus 로고
    • Proximity relationship in the binary complex formed between troponin I and troponin C
    • Wang, C.-K. & Cheung, H. C. (1986) Proximity relationship in the binary complex formed between troponin I and troponin C, J. Mol. Biol. 190, 509-521.
    • (1986) J. Mol. Biol. , vol.190 , pp. 509-521
    • Wang, C.-K.1    Cheung, H.C.2
  • 39
    • 0024473838 scopus 로고
    • 2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex
    • 2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex, Biochemistry 28, 5902-5908.
    • (1989) Biochemistry , vol.28 , pp. 5902-5908
    • Tao, T.1    Gowell, E.2    Strasburg, G.M.3    Gergely, J.4    Leavis, P.C.5
  • 40
    • 0025356099 scopus 로고
    • Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments
    • Tao, T., Gong, B.-J. & 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
  • 41
    • 0029088936 scopus 로고
    • Structures of the tropoinn C regulatory domains in the apo and calcium-saturated states
    • Gagné, S. M., Tsuda, S., Li, M. X., Smillie, L. B. & Sykes, B. D. (1995) Structures of the tropoinn C regulatory domains in the apo and calcium-saturated states, Nat. Struct. Biol. 2, 784-789.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 784-789
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 42
    • 0028342760 scopus 로고
    • The regulatory switch of the muscle thin filament
    • Lehrer, S. S. (1994) The regulatory switch of the muscle thin filament, J. Muscle Res. Cell Motil. 15, 232-236.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 232-236
    • Lehrer, S.S.1
  • 43
    • 0023845153 scopus 로고
    • Structure-function studies of the amino-terminal region of bovine cardiac troponin T
    • Tobacman, L. S. (1988) Structure-function studies of the amino-terminal region of bovine cardiac troponin T, J. Biol. Chem. 263, 2668-2672.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2668-2672
    • Tobacman, L.S.1
  • 44
    • 0025887097 scopus 로고
    • 2-terminal residues of rabbit skeletal troponin T strengthens binding of troponin to immobilized tropomyosin
    • 2-terminal residues of rabbit skeletal troponin T strengthens binding of troponin to immobilized tropomyosin, J. Biol. Chem. 266, 12432-12438.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12432-12438
    • Pan, B.-S.1    Gordon, A.M.2    Potter, J.D.3
  • 45
    • 0030938554 scopus 로고    scopus 로고
    • Production, crystallization and preliminary x-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment(1-47) of troponin I
    • Saijo, Y., Takeda, S., Scherer, A., Kobayashi, T., Maéda, Y., Taniguchi, H., Yao, M. & Wakatsuki, S. (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.
    • (1997) Protein Sci. , vol.6 , pp. 916-918
    • Saijo, Y.1    Takeda, S.2    Scherer, A.3    Kobayashi, T.4    Maéda, Y.5    Taniguchi, H.6    Yao, M.7    Wakatsuki, S.8
  • 46
    • 0026444089 scopus 로고
    • Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone for troponin I
    • Sheng, Z., Pan, B.-S., Miller, T. E. & Potter, J. D. (1992) Isolation, expression, and mutation of a rabbit skeletal muscle cDNA clone for troponin I, J. Biol. Chem. 267, 25407-25413.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25407-25413
    • Sheng, Z.1    Pan, B.-S.2    Miller, T.E.3    Potter, J.D.4
  • 47
    • 0027298766 scopus 로고
    • E. coli expression and characterization of a mutant troponin I with the three cysteine residues substituted
    • Kluwe, L., Maeda, K. & Maéda, Y. (1993) E. coli expression and characterization of a mutant troponin I with the three cysteine residues substituted, FEBS Lett. 323, 83-88.
    • (1993) FEBS Lett. , vol.323 , pp. 83-88
    • Kluwe, L.1    Maeda, K.2    Maéda, Y.3


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