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Volumn 101, Issue 3, 2011, Pages 709-717

Electron microscopy and X-ray diffraction evidence for two Z-band structural states

Author keywords

[No Author keywords available]

Indexed keywords

ALUMINUM DERIVATIVE; ALUMINUM FLUORIDE; CALCIUM; FLUORIDE; TROPONIN C; VANADIC ACID;

EID: 80052501020     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.06.024     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 75749136013 scopus 로고    scopus 로고
    • The vertebrate muscle Z-disc: Sarcomere anchor for structure and signalling
    • P.K. Luther The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling J. Muscle Res. Cell Motil. 30 2009 171 185
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 171-185
    • Luther, P.K.1
  • 2
    • 1242320058 scopus 로고    scopus 로고
    • At the Crossroads of Myocardial Signaling: The Role of Z-Discs in Intracellular Signaling and Cardiac Function
    • DOI 10.1161/01.RES.0000116143.74830.A9
    • W.G. Pyle, and R.J. Solaro At the crossroads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function Circ. Res. 94 2004 296 305 (Pubitemid 38240720)
    • (2004) Circulation Research , vol.94 , Issue.3 , pp. 296-305
    • Pyle, W.G.1    Solaro, R.J.2
  • 3
    • 0014704151 scopus 로고
    • The influence of fixation upon the fine structure of the Z-disk of rat striated muscle
    • D.N. Landon The influence of fixation upon the fine structure of the Z-disk of rat striated muscle J. Cell Sci. 6 1970 257 276
    • (1970) J. Cell Sci. , vol.6 , pp. 257-276
    • Landon, D.N.1
  • 4
    • 0015007428 scopus 로고
    • Observations on organization of Z-disk components and on rod-bodies of Z-disk origin
    • R.D. Macdonald, and A.G. Engel Observations on organization of Z-disk components and on rod-bodies of Z-disk origin J. Cell Biol. 48 1971 431 437
    • (1971) J. Cell Biol. , vol.48 , pp. 431-437
    • MacDonald, R.D.1    Engel, A.G.2
  • 5
    • 0014912922 scopus 로고
    • Change in Z-disk structure with muscular contraction
    • D.N. Landon Change in Z-disk structure with muscular contraction J. Physiol. 211 1970 44 45
    • (1970) J. Physiol. , vol.211 , pp. 44-45
    • Landon, D.N.1
  • 8
    • 0023584297 scopus 로고
    • Z band dynamics as a function of sarcomere length and the contractile state of muscle
    • M.A. Goldstein, and L.H. Michael R.L. Sass Z band dynamics as a function of sarcomere length and the contractile state of muscle FASEB J. 1 1987 133 142 (Pubitemid 18057332)
    • (1987) FASEB Journal , vol.1 , Issue.2 , pp. 133-142
    • Goldstein, M.A.1    Michael, L.H.2    Schroeter, J.P.3    Sass, R.L.4
  • 9
    • 0031725438 scopus 로고    scopus 로고
    • Z/I and A-band lattice spacings in frog skeletal muscle: Effects of contraction and osmolarity
    • DOI 10.1023/A:1005459605964
    • T.C. Irving, and Q. Li B.M. Millman Z/I and A-band lattice spacings in frog skeletal muscle: effects of contraction and osmolarity J. Muscle Res. Cell Motil. 19 1998 811 823 (Pubitemid 28502399)
    • (1998) Journal of Muscle Research and Cell Motility , vol.19 , Issue.7 , pp. 811-823
    • Irving, T.C.1    Li, Q.2    Williams, B.A.3    Millman, B.M.4
  • 10
    • 0023032843 scopus 로고
    • Perfusion cuvette for the simultaneous measurement of mechanical, optical and energetic parameters of skinned muscle fibres
    • DOI 10.1007/BF00657515
    • K. Güth, and R. Wojciechowski Perfusion cuvette for the simultaneous measurement of mechanical, optical and energetic parameters of skinned muscle fibres Pflugers Arch. 407 1986 552 557 (Pubitemid 17175050)
    • (1986) Pflugers Archiv European Journal of Physiology , vol.407 , Issue.5 , pp. 552-557
    • Guth, R.1    Wojciechowski, R.2
  • 11
    • 0014674467 scopus 로고
    • Tropomyosin: Crystal structure, polymorphism and molecular interactions
    • D.L. Caspar, C. Cohen, and W. Longley Tropomyosin: crystal structure, polymorphism and molecular interactions J. Mol. Biol. 41 1969 87 107
    • (1969) J. Mol. Biol. , vol.41 , pp. 87-107
    • Caspar, D.L.1    Cohen, C.2    Longley, W.3
  • 12
    • 0024518455 scopus 로고
    • Structures of actomyosin crossbridges in relaxed and rigor muscle fibers
    • L.C. Yu, and B. Brenner Structures of actomyosin crossbridges in relaxed and rigor muscle fibers Biophys. J. 55 1989 441 453 (Pubitemid 19073739)
    • (1989) Biophysical Journal , vol.55 , Issue.3 , pp. 441-453
    • Yu, L.C.1    Brenner, B.2
  • 13
    • 0022259764 scopus 로고
    • Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture
    • DOI 10.1016/0022-2836(85)90308-0
    • M. Yamaguchi, and M. Izumimoto M.H. Stromer Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture J. Mol. Biol. 184 1985 621 643 (Pubitemid 15024769)
    • (1985) Journal of Molecular Biology , vol.184 , Issue.4 , pp. 621-643
    • Yamaguchi, M.1    Izumimoto, M.2    Robson, R.M.3    Stromer, M.H.4
  • 14
    • 0026534068 scopus 로고
    • Z-line/I-band and A-band lattices of intact frog sartorius muscle at altered interfilament spacing
    • T.C. Irving, and B.M. Millman Z-line/I-band and A-band lattices of intact frog sartorius muscle at altered interfilament spacing J. Muscle Res. Cell Motil. 13 1992 100 105
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 100-105
    • Irving, T.C.1    Millman, B.M.2
  • 15
    • 0021150823 scopus 로고
    • X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths
    • B. Brenner, L.C. Yu, and R.J. Podolsky X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths Biophys. J. 46 1984 299 306 (Pubitemid 14046111)
    • (1984) Biophysical Journal , vol.46 , Issue.3 , pp. 299-306
    • Brenner, B.1    Yu, L.C.2    Podolsky, R.J.3
  • 16
    • 0020583740 scopus 로고
    • Co-ordinated electron microscopy and X-ray studies of glycerinated insect flight muscle. I. X-ray diffraction monitoring during preparation for electron microscopy of muscle fibres fixed in rigor, in ATP and in AMPPNP
    • M.K. Reedy, and R.S. Goody G. Rosenbaum Co-ordinated electron microscopy and x-ray studies of glycerinated insect flight muscle. I. X-ray diffraction monitoring during preparation for electron microscopy of muscle fibres fixed in rigor, in ATP and in AMPPNP J. Muscle Res. Cell Motil. 4 1983 25 53 (Pubitemid 13133757)
    • (1983) Journal of Muscle Research and Cell Motility , vol.4 , Issue.1 , pp. 25-53
    • Reedy, M.K.1    Goody, R.S.2    Hofmann, W.3    Rosenbaum, G.4
  • 17
    • 0020536686 scopus 로고
    • Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers
    • B. Brenner Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers Biophys. J. 41 1983 99 102 (Pubitemid 13114326)
    • (1983) Biophysical Journal , vol.41 , Issue.1 , pp. 99-102
    • Brenner, B.1
  • 19
    • 0023187156 scopus 로고
    • Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle
    • DOI 10.1016/0022-2836(87)90492-X
    • P.W. Brandt, and M.S. Diamond F.H. Schachat Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle J. Mol. Biol. 195 1987 885 896 (Pubitemid 17095063)
    • (1987) Journal of Molecular Biology , vol.195 , Issue.4 , pp. 885-896
    • Brandt, P.W.1    Diamond, M.S.2    Rutchik, J.S.3    Schachat, F.H.4
  • 20
    • 0027407920 scopus 로고
    • Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit
    • P.B. Chase, and D.A. Martyn A.M. Gordon Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibres from rabbit J. Physiol. 460 1993 231 246 (Pubitemid 23058048)
    • (1993) Journal of Physiology , vol.460 , pp. 231-246
    • Chase, P.B.1    Martyn, D.A.2    Kushmerick, M.J.3    Gordon, A.M.4
  • 21
    • 0036297519 scopus 로고    scopus 로고
    • The three-dimensional structure of a vertebrate wide (slow muscle) Z-band: Lessons on Z-band assembly
    • DOI 10.1006/jmbi.2001.5217
    • P.K. Luther, J.S. Barry, and J.M. Squire The three-dimensional structure of a vertebrate wide (slow muscle) Z-band: lessons on Z-band assembly J. Mol. Biol. 315 2002 9 20 (Pubitemid 34722108)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.1 , pp. 9-20
    • Luther, P.K.1    Barry, J.S.2    Squire, J.M.3
  • 22
    • 0025606398 scopus 로고
    • The three-dimensional structure of the nemaline rod Z-band
    • E.P. Morris, G. Nneji, and J.M. Squire The three-dimensional structure of the nemaline rod Z-band J. Cell Biol. 111 1990 2961 2978 (Pubitemid 120034035)
    • (1990) Journal of Cell Biology , vol.111 , Issue.6 PART 2 , pp. 2961-2978
    • Morris, E.P.1    Nneji, G.2    Squire, J.M.3
  • 24
    • 0035919832 scopus 로고    scopus 로고
    • 2+-dependent actin binding
    • DOI 10.1006/jmbi.2001.4789
    • J. Tang, D.W. Taylor, and K.A. Taylor The three-dimensional structure of alpha-actinin obtained by cryoelectron microscopy suggests a model for Ca(2+)-dependent actin binding J. Mol. Biol. 310 2001 845 858 (Pubitemid 32695699)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.4 , pp. 845-858
    • Tang, J.1    Taylor, D.W.2    Taylor, K.A.3
  • 25
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the α-actinin rod reveals an extensive torsional twist
    • DOI 10.1016/S0969-2126(01)00619-0, PII S0969212601006190
    • J. Ylänne, and K. Scheffzek M. Saraste Crystal structure of the alpha-actinin rod reveals an extensive torsional twist Structure 9 2001 597 604 (Pubitemid 32695584)
    • (2001) Structure , vol.9 , Issue.7 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 26
    • 67049146466 scopus 로고    scopus 로고
    • Molecular mechanics of the alpha-actinin rod domain: Bending, torsional, and extensional behavior
    • J. Golji, R. Collins, and M.R. Mofrad Molecular mechanics of the alpha-actinin rod domain: bending, torsional, and extensional behavior PLOS Comput. Biol. 5 2009 e1000389
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000389
    • Golji, J.1    Collins, R.2    Mofrad, M.R.3
  • 27
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • DOI 10.1093/emboj/17.6.1614
    • P. Young, and C. Ferguson M. Gautel Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin EMBO J. 17 1998 1614 1624 (Pubitemid 28119115)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 28
    • 0025868336 scopus 로고
    • Studies of the α-actinin/actin interaction in the Z-disk by using calpain
    • D.E. Goll, and W.R. Dayton R.M. Robson Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain J. Biol. Chem. 266 1991 8501 8510 (Pubitemid 21906538)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.13 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4
  • 30
    • 0344629442 scopus 로고    scopus 로고
    • Calpain 3 Is Activated through Autolysis within the Active Site and Lyses Sarcomeric and Sarcolemmal Components
    • DOI 10.1128/MCB.23.24.9127-9135.2003
    • M. Taveau, and N. Bourg I. Richard Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components Mol. Cell. Biol. 23 2003 9127 9135 (Pubitemid 37499802)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9127-9135
    • Taveau, M.1    Bourg, N.2    Sillon, G.3    Roudaut, C.4    Bartoli, M.5    Richard, I.6
  • 32
    • 0036389773 scopus 로고    scopus 로고
    • Titin organisation and the 3D architecture of the vertebrate-striated muscle I-band
    • C. Knupp, P.K. Luther, and J.M. Squire Titin organisation and the 3D architecture of the vertebrate-striated muscle I-band J. Mol. Biol. 322 2002 731 739
    • (2002) J. Mol. Biol. , vol.322 , pp. 731-739
    • Knupp, C.1    Luther, P.K.2    Squire, J.M.3
  • 33
    • 0036301051 scopus 로고    scopus 로고
    • Muscle Z-band ultrastructure: Titin Z-repeats and Z-band periodicities do not match
    • DOI 10.1016/S0022-2836(02)00372-8
    • P.K. Luther, and J.M. Squire Muscle Z-band ultrastructure: titin Z-repeats and Z-band periodicities do not match J. Mol. Biol. 319 2002 1157 1164 (Pubitemid 34729425)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1157-1164
    • Luther, P.K.1    Squire, J.M.2
  • 34
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • S.N. Timasheff The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22 1993 67 97 (Pubitemid 23180317)
    • (1993) Annual Review of Biophysics and Biomolecular Structure , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 35
    • 0030756203 scopus 로고    scopus 로고
    • Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and to protein-protein association
    • C.J. Tsai, and R. Nussinov Hydrophobic folding units at protein-protein interfaces: implications to protein folding and to protein-protein association Protein Sci. 6 1997 1426 1437
    • (1997) Protein Sci. , vol.6 , pp. 1426-1437
    • Tsai, C.J.1    Nussinov, R.2
  • 36
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-protein interactions: What are the preferred ways for proteins to interact?
    • DOI 10.1021/cr040409x
    • O. Keskin, and A. Gursoy R. Nussinov Principles of protein-protein interactions: what are the preferred ways for proteins to interact? Chem. Rev. 108 2008 1225 1244 (Pubitemid 351638814)
    • (2008) Chemical Reviews , vol.108 , Issue.4 , pp. 1225-1244
    • Keskin, O.1    Gursoy, A.2    Ma, B.3    Nussinov, R.4
  • 37
    • 0014597040 scopus 로고
    • Some properties of chicken alpha-actinin
    • T. Masaki, and O. Takaiti Some properties of chicken alpha-actinin J. Biochem. 66 1969 637 643
    • (1969) J. Biochem. , vol.66 , pp. 637-643
    • Masaki, T.1    Takaiti, O.2
  • 38
    • 0017146229 scopus 로고
    • Some properties of purified skeletal muscle alpha-actinin
    • A. Suzuki, and D.E. Goll M.H. Stromer Some properties of purified skeletal muscle alpha-actinin J. Biol. Chem. 251 1976 6860 6870
    • (1976) J. Biol. Chem. , vol.251 , pp. 6860-6870
    • Suzuki, A.1    Goll, D.E.2    Stromer, M.H.3
  • 39
    • 33747767574 scopus 로고    scopus 로고
    • A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle
    • DOI 10.1016/j.jsb.2006.02.020, PII S1047847706001080, Fibrous Protein Structure
    • K.J. Poole, and M. Lorenz K.C. Holmes A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle x-ray fibre diagrams from non-overlap muscle J. Struct. Biol. 155 2006 273 284 (Pubitemid 44278649)
    • (2006) Journal of Structural Biology , vol.155 , Issue.2 , pp. 273-284
    • Poole, K.J.V.1    Lorenz, M.2    Evans, G.3    Rosenbaum, G.4    Pirani, A.5    Craig, R.6    Tobacman, L.S.7    Lehman, W.8    Holmes, K.C.9
  • 41
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • DOI 10.1006/jmbi.1996.0800
    • P. Vibert, R. Craig, and W. Lehman Steric-model for activation of muscle thin filaments J. Mol. Biol. 266 1997 8 14 (Pubitemid 27170513)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.1 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 42
    • 73149102752 scopus 로고    scopus 로고
    • The shape and flexibility of tropomyosin coiled coils: Implications for actin filament assembly and regulation
    • X.E. Li, and K.C. Holmes S. Fischer The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation J. Mol. Biol. 395 2010 327 339
    • (2010) J. Mol. Biol. , vol.395 , pp. 327-339
    • Li, X.E.1    Holmes, K.C.2    Fischer, S.3
  • 43
    • 0022239695 scopus 로고
    • The presence of two skeletal muscle α-actinins correlates with troponin-tropomyosin expression and Z-line width
    • DOI 10.1083/jcb.101.3.1001
    • F.H. Schachat, and A.C. Canine M.C. Reedy The presence of two skeletal muscle alpha-actinins correlates with troponin-tropomyosin expression and Z-line width J. Cell Biol. 101 1985 1001 1008 (Pubitemid 16258227)
    • (1985) Journal of Cell Biology , vol.101 , Issue.3 , pp. 1001-1008
    • Schachat, F.H.1    Canine, A.C.2    Briggs, M.M.3    Reedy, M.C.4
  • 44
    • 0028852835 scopus 로고
    • A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy
    • N.G. Laing, and S.D. Wilton E. Haan A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy Nat. Genet. 9 1995 75 79
    • (1995) Nat. Genet. , vol.9 , pp. 75-79
    • Laing, N.G.1    Wilton, S.D.2    Haan, E.3
  • 46
    • 3242741080 scopus 로고    scopus 로고
    • Evidence for a direct but sequential binding of titin to tropomyosin and actin filaments
    • DOI 10.1016/j.bbapap.2004.05.001, PII S1570963904001396
    • F. Raynaud, C. Astier, and Y. Benyamin Evidence for a direct but sequential binding of titin to tropomyosin and actin filaments Biochim. Biophys. Acta 1700 2004 171 178 (Pubitemid 38950703)
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1700 , Issue.2 , pp. 171-178
    • Raynaud, F.1    Astier, C.2    Benyamin, Y.3
  • 47
    • 0015236791 scopus 로고
    • N lines in striated muscle: A site of intracellular Ca2+
    • R. Yarom, and U. Meiri N lines in striated muscle: a site of intracellular Ca2+ Nat. New Biol. 234 1971 254 256
    • (1971) Nat. New Biol. , vol.234 , pp. 254-256
    • Yarom, R.1    Meiri, U.2
  • 48
    • 0024435232 scopus 로고
    • Ultrastructural localization of calcium in post-mortem bovine muscle: A cytochemical and X-ray microanalytical study
    • X. Vignon, J. Beaulaton, and A. Ouali Ultrastructural localization of calcium in post-mortem bovine muscle: a cytochemical and x-ray microanalytical study Histochem. J. 21 1989 403 411 (Pubitemid 19228310)
    • (1989) Histochemical Journal , vol.21 , Issue.7 , pp. 403-411
    • Vignon, X.1    Beaulaton, J.2    Ouali, A.3
  • 49
    • 50849095774 scopus 로고    scopus 로고
    • Calpain 1 binding capacities of the N1-line region of titin are significantly enhanced by physiological concentrations of calcium
    • G. Coulis, and S. Becila A. Ouali Calpain 1 binding capacities of the N1-line region of titin are significantly enhanced by physiological concentrations of calcium Biochemistry 47 2008 9174 9183
    • (2008) Biochemistry , vol.47 , pp. 9174-9183
    • Coulis, G.1    Becila, S.2    Ouali, A.3
  • 50
    • 18944385186 scopus 로고    scopus 로고
    • Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril
    • DOI 10.1111/j.1742-4658.2005.04683.x
    • F. Raynaud, and E. Fernandez A. Ouali Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril FEBS J. 272 2005 2578 2590 (Pubitemid 40705077)
    • (2005) FEBS Journal , vol.272 , Issue.10 , pp. 2578-2590
    • Raynaud, F.1    Fernandez, E.2    Coulis, G.3    Aubry, L.4    Vignon, X.5    Bleimling, N.6    Gautel, M.7    Benyamin, Y.8    Ouali, A.9


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