메뉴 건너뛰기




Volumn 38, Issue 1, 2006, Pages 110-122

Ca2+ and Mg2+ binding to weak sites of TnC C-domain induces exposure of a large hydrophobic surface that leads to loss of TnC from the thin filament

Author keywords

bis ANS; Divalent cations; F154W C domain; Troponin C; Tryptophan fluorescence

Indexed keywords

CALCIUM; MAGNESIUM; PHENYLALANINE; PROTEIN SUBUNIT; SULFONIC ACID DERIVATIVE; TROPONIN C;

EID: 27544511447     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2005.08.009     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0019875920 scopus 로고
    • 25Mg NMR study of rabbit skeletal muscle troponin C: Exchange rates and binding constants
    • 25Mg NMR study of rabbit skeletal muscle troponin C: Exchange rates and binding constants FEBS Lett. 125 1981 39 43
    • (1981) FEBS Lett. , vol.125 , pp. 39-43
    • Andersson, T.1    Drakenberg, T.2    Forsen, S.3    Thulin, E.4
  • 3
    • 0028176943 scopus 로고
    • 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C
    • 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C Biochemistry 33 1994 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
  • 4
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • C.S. Farah, and F.C. Reinach The troponin complex and regulation of muscle contraction FASEB J. 9 1995 755 767
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 8
    • 0020334193 scopus 로고
    • Free magnesium in sheep, ferret and frog striated muscle at rest measured with ion-selective micro-electrodes
    • P. Hess, P. Metzger, and R. Weingart Free magnesium in sheep, ferret and frog striated muscle at rest measured with ion-selective micro-electrodes J. Physiol. 333 1982 173 188
    • (1982) J. Physiol. , vol.333 , pp. 173-188
    • Hess, P.1    Metzger, P.2    Weingart, R.3
  • 9
    • 0018142608 scopus 로고
    • Calcium-binding properties of cardiac and skeletal troponin C as determined by circular dichroism and ultraviolet difference spectroscopy
    • M.T. Hincke, W.D. McCubbin, and C.M. Kay Calcium-binding properties of cardiac and skeletal troponin C as determined by circular dichroism and ultraviolet difference spectroscopy Can. J. Biochem. 56 1978 384 395
    • (1978) Can. J. Biochem. , vol.56 , pp. 384-395
    • Hincke, M.T.1    McCubbin, W.D.2    Kay, C.M.3
  • 12
    • 17744382824 scopus 로고    scopus 로고
    • Structural based insights into the role of troponin in cardiac muscle pathophysiology
    • M.X. Li, X. Wang, and B. Sykes Structural based insights into the role of troponin in cardiac muscle pathophysiology J. Muscle Res. Cell Motil. 25 2004 559 579
    • (2004) J. Muscle Res. Cell Motil. , vol.25 , pp. 559-579
    • Li, M.X.1    Wang, X.2    Sykes, B.3
  • 14
    • 0033554429 scopus 로고    scopus 로고
    • Optical spectroscopic characterization of single tryptophan mutants of chicken skeletal troponin C: Evidence for interdomain interaction
    • M.C. Moncrieffe, S.Y. Venyaminov, T.E. Miller, G. Guzman, J.D. Potter, and F.G. Prendergast Optical spectroscopic characterization of single tryptophan mutants of chicken skeletal troponin C: Evidence for interdomain interaction Biochemistry 38 1999 11973 11983
    • (1999) Biochemistry , vol.38 , pp. 11973-11983
    • Moncrieffe, M.C.1    Venyaminov, S.Y.2    Miller, T.E.3    Guzman, G.4    Potter, J.D.5    Prendergast, F.G.6
  • 16
    • 0038375332 scopus 로고    scopus 로고
    • The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I
    • D.C. Oliveira, and F.C. Reinach The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I Eur. J. Biochem. 270 2003 2937 2944
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2937-2944
    • Oliveira, D.C.1    Reinach, F.C.2
  • 17
    • 0028170185 scopus 로고
    • 2+ sensitivity of mammalian skinned cardiac and skeletal muscle fibres
    • 2+ sensitivity of mammalian skinned cardiac and skeletal muscle fibres J. Physiol. 480 1994 45 60
    • (1994) J. Physiol. , vol.480 , pp. 45-60
    • Palmer, S.1    Kentish, J.C.2
  • 18
    • 0008392486 scopus 로고    scopus 로고
    • Interaction of cardiotonic thiadiazinone derivatives with cardiac troponin C
    • B. Pan, and R.G. Johnson Jr. Interaction of cardiotonic thiadiazinone derivatives with cardiac troponin C J. Biol. Chem. 271 1996 817 823
    • (1996) J. Biol. Chem. , vol.271 , pp. 817-823
    • Pan, B.1    Johnson Jr., R.G.2
  • 20
    • 0031003385 scopus 로고    scopus 로고
    • Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I
    • J.R. Pearlstone, B.D. Sykes, and L.B. Smillie Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I Biochemistry 36 1997 7601 7606
    • (1997) Biochemistry , vol.36 , pp. 7601-7606
    • Pearlstone, J.R.1    Sykes, B.D.2    Smillie, L.B.3
  • 21
    • 0027138871 scopus 로고
    • Aluminum fluoride interactions with troponin C
    • B.C. Phan, and E. Reisler Aluminum fluoride interactions with troponin C Biophys. J. 65 1993 2511 2516
    • (1993) Biophys. J. , vol.65 , pp. 2511-2516
    • Phan, B.C.1    Reisler, E.2
  • 22
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biomol. NMR 2 1992 661 665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 23
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • J.D. Potter, and J. Gergely 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
  • 24
    • 0014589353 scopus 로고
    • Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. a new fluorescent molecule with exceptional binding properties
    • G. Rosen, and G. Weber Dimer formation from 1-amino-8- naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties Biochemistry 8 1969 3915 3920
    • (1969) Biochemistry , vol.8 , pp. 3915-3920
    • Rosen, G.1    Weber, G.2
  • 25
    • 0025644197 scopus 로고
    • Evidence that both Ca(2+)-specific sites of skeletal muscle TnC are required for full activity
    • Z. Sheng, W.L. Strauss, J.M. Francois, and J.D. Potter Evidence that both Ca(2+)-specific sites of skeletal muscle TnC are required for full activity J. Biol. Chem. 265 1990 21554 21560
    • (1990) J. Biol. Chem. , vol.265 , pp. 21554-21560
    • Sheng, Z.1    Strauss, W.L.2    Francois, J.M.3    Potter, J.D.4
  • 26
    • 0029077856 scopus 로고
    • Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy
    • C.M. Slupsky, F.C. Reinach, L.B. Smillie, and B.D. Sykes Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy Prot. Sci. 4 1995 1279 1290
    • (1995) Prot. Sci. , vol.4 , pp. 1279-1290
    • Slupsky, C.M.1    Reinach, F.C.2    Smillie, L.B.3    Sykes, B.D.4
  • 27
    • 0035836456 scopus 로고    scopus 로고
    • The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL
    • A.L. Smoot, M. Panda, B.T. Brazil, A.M. Buckle, A.R. Fersht, and P.M. Horowitz The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL Biochemistry 40 2001 4484 4492
    • (2001) Biochemistry , vol.40 , pp. 4484-4492
    • Smoot, A.L.1    Panda, M.2    Brazil, B.T.3    Buckle, A.M.4    Fersht, A.R.5    Horowitz, P.M.6
  • 28
    • 0022517661 scopus 로고
    • Caffeine inhibition of calcium accumulation by the sarcoplasmic reticulum in mammalian skinned fibers
    • M.M. Sorenson, H.S.L. Coelho, and J.P. Reuben Caffeine inhibition of calcium accumulation by the sarcoplasmic reticulum in mammalian skinned fibers J. Membr. Biol. 90 1986 219 230
    • (1986) J. Membr. Biol. , vol.90 , pp. 219-230
    • Sorenson, M.M.1    Coelho, H.S.L.2    Reuben, J.P.3
  • 29
  • 32
    • 0026728168 scopus 로고
    • A comparative spectroscopic study of tryptophan probes engineered into high- and low-affinity domains of recombinant chicken troponin C
    • G. Trigo-Gonzalez, K. Racher, L. Burtnick, and T. Borgford A comparative spectroscopic study of tryptophan probes engineered into high- and low-affinity domains of recombinant chicken troponin C Biochemistry 31 1992 7009 7015
    • (1992) Biochemistry , vol.31 , pp. 7009-7015
    • Trigo-Gonzalez, G.1    Racher, K.2    Burtnick, L.3    Borgford, T.4
  • 35
    • 0026615878 scopus 로고
    • 2+ concentration during repetitive stimulation of single fibres from mouse skeletal muscle
    • 2+ concentration during repetitive stimulation of single fibres from mouse skeletal muscle J. Physiol. 453 1992 413 434
    • (1992) J. Physiol. , vol.453 , pp. 413-434
    • Westerblad, H.1    Allen, D.G.2
  • 36
    • 0020000247 scopus 로고
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils
    • 2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils J. Biol. Chem. 257 1982 7678 7683
    • (1982) J. Biol. Chem. , vol.257 , pp. 7678-7683
    • Zot, H.G.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.