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Volumn 270, Issue 14, 2003, Pages 2937-2944

The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I

Author keywords

5 hydroxytryptophan; Ca2+ binding protein; Fluorescence; Skeletal muscle; Troponin

Indexed keywords

AMINO ACID; CALCIUM ION; MUTANT PROTEIN; TROPONIN; TROPONIN I;

EID: 0038375332     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03659.x     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 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
  • 2
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire, J.M. & Morris, E.P. (1998) A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12, 761-771.
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 3
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A.M., Homsher, E. & 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
  • 4
    • 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
  • 5
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrilar adenosine triphosphatase
    • Potter, J.D. & Gergely, J. (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrilar adenosine triphosphatase. J. Biol. Chem. 250, 4628-4633.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 8
    • 0032562290 scopus 로고    scopus 로고
    • 2- and COOH-terminal domains of troponin T: ATPase activation and binding to troponin I and troponin C
    • 2- and COOH-terminal domains of troponin T: ATPase activation and binding to troponin I and troponin C. J. Biol. Chem. 273, 10594-10601.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10594-10601
    • Malnic, B.1    Farah, C.S.2    Reinach, F.C.3
  • 9
    • 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. & Maeda, Y. (1998) Crystal structure of troponin C in complex with troponin I fragment at 2.3-Å resolution. Proc. Natl Acad. Sci. USA 95, 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    Maeda, Y.5
  • 10
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit
    • Syska, H., Wilkinson, J.M., Grand, R.J.A. & Perry, S.V. (1976) The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Bichem. J. 153, 375-387.
    • (1976) Bichem. J. , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.A.3    Perry, S.V.4
  • 11
    • 0026670753 scopus 로고
    • A new intrinsic fluorescent probe for proteins
    • Hogue, C.W.V., Rasquinha, I., Szabo, A.G. & MacManus, J.P. (1992) A new intrinsic fluorescent probe for proteins. FEBS 310, 269-272.
    • (1992) FEBS , vol.310 , pp. 269-272
    • Hogue, C.W.V.1    Rasquinha, I.2    Szabo, A.G.3    MacManus, J.P.4
  • 12
    • 0033543220 scopus 로고    scopus 로고
    • 2+-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site
    • 2+-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site. Biochemistry 38, 10543-10551.
    • (1999) Biochemistry , vol.38 , pp. 10543-10551
    • Farah, C.S.1    Reinach, F.C.2
  • 13
    • 0022432255 scopus 로고
    • Improved oligonucleotide site-directed mutagenesis using M13 vectors
    • Carter, P., Bedouelle, H. & Winter, G. (1985) Improved oligonucleotide site-directed mutagenesis using M13 vectors. Nucleic Acids Res. 13, 4431-4443.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 4431-4443
    • Carter, P.1    Bedouelle, H.2    Winter, G.3
  • 14
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D. & Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 15
    • 0027197251 scopus 로고
    • Cloning and expression of chicken skeletal muscle troponin I in Escherichia coli: The role of rare codons on the expression level
    • Quaggio, R.B., Ferro, J.A., Monteiro, P.B. & Reinach, F.C. (1993) Cloning and expression of chicken skeletal muscle troponin I in Escherichia coli: The role of rare codons on the expression level. Protein Sci. 2, 1053-1056.
    • (1993) Protein Sci. , vol.2 , pp. 1053-1056
    • Quaggio, R.B.1    Ferro, J.A.2    Monteiro, P.B.3    Reinach, F.C.4
  • 19
    • 0014433049 scopus 로고
    • Amino acid replacements of the glutamic acid residue at position 48 in tryptophan synthetase A of Escherichia coli
    • Drapeau, G.R., Brammar, W.J. & Yanofsky, C. (1968) Amino acid replacements of the glutamic acid residue at position 48 in tryptophan synthetase A of Escherichia coli. J. Mol. Biol. 35, 357-367.
    • (1968) J. Mol. Biol. , vol.35 , pp. 357-367
    • Drapeau, G.R.1    Brammar, W.J.2    Yanofsky, C.3
  • 21
    • 0025270821 scopus 로고
    • Probing the calcium-induced conformational transition of troponin C with site-directed mutants
    • Fujimori, K., Sorenson, M., Herzberg, O., Moult, J. & Reinach, F.C. (1990) Probing the calcium-induced conformational transition of troponin C with site-directed mutants. Nature 345, 182-184.
    • (1990) Nature , vol.345 , pp. 182-184
    • Fujimori, K.1    Sorenson, M.2    Herzberg, O.3    Moult, J.4    Reinach, F.C.5
  • 22
    • 0015994735 scopus 로고
    • The interaction of the calcium binding troponin (troponin C) with bivalent cations and the inhibitory protein (troponin 1)
    • Head, J.F. & Perry, S.V. (1974) The interaction of the calcium binding troponin (troponin C) with bivalent cations and the inhibitory protein (troponin 1). Biochem. J. 137, 145-154.
    • (1974) Biochem. J. , vol.137 , pp. 145-154
    • Head, J.F.1    Perry, S.V.2
  • 23
    • 0015384891 scopus 로고
    • Determination of protein: A modification of Lowry method that gives a linear photometric response
    • Hartree, E.F. (1972) Determination of protein: a modification of Lowry method that gives a linear photometric response. Anal. Biochem. 4, 422-427.
    • (1972) Anal. Biochem. , vol.4 , pp. 422-427
    • Hartree, E.F.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of the bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of head of the bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0028310127 scopus 로고
    • A practical guide to the preparation of Ca2+ buffers
    • Bers, D.M., Patton, C.W. & Nuccitelli, R. (1994) A practical guide to the preparation of Ca2+ buffers. Methods Cell Biol. 40, 3-29.
    • (1994) Methods Cell Biol. , vol.40 , pp. 3-29
    • Bers, D.M.1    Patton, C.W.2    Nuccitelli, R.3
  • 26
    • 0024211683 scopus 로고
    • Sequences of complete cDNAs encoding four variants of chicken skeletal muscle troponin T
    • Smillie, L.B., Golosinska, K. & Reinach, F.C. (1988) Sequences of complete cDNAs encoding four variants of chicken skeletal muscle troponin T. J. Biol. Chem. 263, 18816-18820.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18816-18820
    • Smillie, L.B.1    Golosinska, K.2    Reinach, F.C.3
  • 27
    • 0023859144 scopus 로고
    • Cloning, expression and site-directed mutagenesis of chicken skeletal muscle troponin C
    • Reinach, F.C. & Karlsson, R. (1988) Cloning, expression and site-directed mutagenesis of chicken skeletal muscle troponin C. J. Biol. Chem. 263, 2371-2376.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2371-2376
    • Reinach, F.C.1    Karlsson, R.2
  • 28
    • 0033603297 scopus 로고    scopus 로고
    • Mapping subdomains in the C-terminal region of troponin I involved in its binding to troponin C and thin filament
    • Ramos, C.H.I. (1999) Mapping subdomains in the C-terminal region of troponin I involved in its binding to troponin C and thin filament. J. Biol. Chem. 274, 18189-18195.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18189-18195
    • Ramos, C.H.I.1
  • 31
    • 0025644197 scopus 로고
    • Evidence that both Ca (2+) -specific sites of skeletal muscle TnC are required for full activity
    • Sheng, Z., Strauss, W.L., François, J.M. & Potter, J.D. (1990) Evidence that both Ca (2+) -specific sites of skeletal muscle TnC are required for full activity. J. Biol. Chem. 265, 21554-21660.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21554-21660
    • Sheng, Z.1    Strauss, W.L.2    François, J.M.3    Potter, J.D.4
  • 32
    • 0021918919 scopus 로고
    • Kinetic studies of calcium and magnesium binding to troponin C
    • Rosenfeld, S.S. & Taylor, E.W. (1985) Kinetic studies of calcium and magnesium binding to troponin C. J. Biol. Chem. 260, 242-251.
    • (1985) J. Biol. Chem. , vol.260 , pp. 242-251
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 33
    • 0022606964 scopus 로고
    • Calcium binding to the low affinity sites in troponin C induces conformational changes in high affinity domain: A possible route of information transfer in activation of muscle contraction
    • Grebarek, Z., Leavis, P.C. & Gergely, J. (1986) Calcium binding to the low affinity sites in troponin C induces conformational changes in high affinity domain: a possible route of information transfer in activation of muscle contraction. J. Biol. Chem. 261, 608-613.
    • (1986) J. Biol. Chem. , vol.261 , pp. 608-613
    • Grebarek, Z.1    Leavis, P.C.2    Gergely, J.3
  • 34
    • 0026530360 scopus 로고
    • Interaction of troponin C and troponin C fragments with troponin I and the troponin I inhibitory peptide
    • Swenson, C.A. & Fredricksen, R.S. (1992) Interaction of troponin C and troponin C fragments with troponin I and the troponin I inhibitory peptide. Biochemistry 31, 3420-3429.
    • (1992) Biochemistry , vol.31 , pp. 3420-3429
    • Swenson, C.A.1    Fredricksen, R.S.2
  • 35
    • 0028176943 scopus 로고
    • 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken muscle troponin C
    • 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken muscle troponin C. Biochemistry 33, 2961-2969.
    • (1994) Biochemistry , vol.33 , pp. 2961-2969
    • Chandra, M.1    McCubbin, W.D.2    Oikawa, K.3    Kay, C.M.4    Smillie, L.B.5
  • 36
    • 0029060203 scopus 로고
    • Evidence for two-site binding of troponin I inhibitory peptides to the N and C Domains of TnC
    • Pearlstone, J.R. & Smillie, L.B. (1995) Evidence for two-site binding of troponin I inhibitory peptides to the N and C Domains of TnC. Biochemistry 34, 6932-6940.
    • (1995) Biochemistry , vol.34 , pp. 6932-6940
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 37
    • 0031003385 scopus 로고    scopus 로고
    • Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I
    • Pearlstone, J.R., Sykes, B.D. & Smillie, L.B. (1997) Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I. Biochemistry 36, 7601-7606.
    • (1997) Biochemistry , vol.36 , pp. 7601-7606
    • Pearlstone, J.R.1    Sykes, B.D.2    Smillie, L.B.3
  • 38
    • 0022931544 scopus 로고
    • 2+ -induced conformational transition of troponin C. A trigger for muscle contraction
    • 2+ -induced conformational transition of troponin C. A trigger for muscle contraction. J. Biol. Chem. 261, 2638-2644.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.N.G.3
  • 39
    • 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. & Sykes, B.D. (1995) Structures of the troponin 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
  • 40
    • 0030952840 scopus 로고    scopus 로고
    • Structural and functional domains of the troponin complex reveled by limited digestion
    • Takeda, S., Kobayashi, T., Taniguchi, H., Hayashi, H. & Maeda, Y. (1997) Structural and functional domains of the troponin complex reveled 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
  • 41
    • 0030692043 scopus 로고    scopus 로고
    • Interaction of the second binding region of troponin I with the regulatory domain of skeletal muscle troponin C as determined by NMR spectroscopy
    • McKay, R.T., Tripet, B.P., Hodges, R.S. & Sykes, B.D. (1997) Interaction of the second binding region of troponin I with the regulatory domain of skeletal muscle troponin C as determined by NMR spectroscopy. J. Biol. Chem. 272, 28494-28500.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28494-28500
    • McKay, R.T.1    Tripet, B.P.2    Hodges, R.S.3    Sykes, B.D.4
  • 42
    • 0033580684 scopus 로고    scopus 로고
    • Residues 48 and 82 at the N-terminal hydrophobic pocket of rabbit skeletal muscle troponin-C photo-cross-link to Met121 of troponin-I
    • Luo, Y., Leszyk, J., Qian, Y., Gergely, J. & Tao, T. (1999) Residues 48 and 82 at the N-terminal hydrophobic pocket of rabbit skeletal muscle troponin-C photo-cross-link to Met121 of troponin-I. Biochemistry 38, 6678-6688.
    • (1999) Biochemistry , vol.38 , pp. 6678-6688
    • Luo, Y.1    Leszyk, J.2    Qian, Y.3    Gergely, J.4    Tao, T.5
  • 44
    • 0036789941 scopus 로고    scopus 로고
    • Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance
    • Brown, L.J., Sale, K.L., Hills, R., Rouviere, C., Song, L., Zhang, X. & Fajer, P.G. (2002) Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance. Proc. Natl Acad. Sci. USA 99, 12765-12770.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12765-12770
    • Brown, L.J.1    Sale, K.L.2    Hills, R.3    Rouviere, C.4    Song, L.5    Zhang, X.6    Fajer, P.G.7
  • 45
    • 0020479286 scopus 로고
    • Study of the structure of troponin I by measuring the relative reactivities of lysines with acetic anhydride
    • Hitchcock-De Gregori, S.E. (1982) Study of the structure of troponin I by measuring the relative reactivities of lysines with acetic anhydride. J. Biol. Chem. 257, 7372-7380.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7372-7380
    • Hitchcock-De Gregori, S.E.1
  • 46
    • 0034711952 scopus 로고    scopus 로고
    • Photocrosslinking of benzophenone-labeled single cysteine troponin I mutants to other thin filament proteins
    • Luo, Y., Wu, J.L., Li, B., Langsetmo, K., Gergely, J. & Tao, T. (2000) Photocrosslinking of benzophenone-labeled single cysteine troponin I mutants to other thin filament proteins. J. Mol. Biol. 296, 899-910.
    • (2000) J. Mol. Biol. , vol.296 , pp. 899-910
    • Luo, Y.1    Wu, J.L.2    Li, B.3    Langsetmo, K.4    Gergely, J.5    Tao, T.6
  • 47
    • 0029946423 scopus 로고    scopus 로고
    • Relationship between stability and function for isolated domains of troponin C
    • Fredricksen, R.S. & Swenson, C.A. (1996) Relationship between stability and function for isolated domains of troponin C. Biochemistry 35, 14012-14026.
    • (1996) Biochemistry , vol.35 , pp. 14012-14026
    • Fredricksen, R.S.1    Swenson, C.A.2
  • 48
    • 0034696575 scopus 로고    scopus 로고
    • 2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I
    • 2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I. Biochemistry 39, 2902-2911.
    • (2000) Biochemistry , vol.39 , pp. 2902-2911
    • Mercier, P.1    Li, M.X.2    Sykes, B.D.3


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