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Volumn 71, Issue 2, 1996, Pages 576-589

Small segmental rearrangements in the myosin head can explain force generation in muscle

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; TROPOMYOSIN;

EID: 0006844340     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79292-5     Document Type: Article
Times cited : (27)

References (59)
  • 1
    • 0027193934 scopus 로고
    • Role of sequence 18-29 on actin in actomyosin interactions
    • Adams, S., and E. Reisler. 1993. Role of sequence 18-29 on actin in actomyosin interactions. Biochemistry. 32:5051-5056.
    • (1993) Biochemistry , vol.32 , pp. 5051-5056
    • Adams, S.1    Reisler, E.2
  • 2
    • 0019945854 scopus 로고
    • Structural evidence that myosin heads may interact with two sites on F-actin
    • Amos, L. A., H. E. Huxley, K. C. Holmes, R. S. Goody, and K. A. Taylor. 1982. Structural evidence that myosin heads may interact with two sites on F-actin. Nature. 299:467-469.
    • (1982) Nature , vol.299 , pp. 467-469
    • Amos, L.A.1    Huxley, H.E.2    Holmes, K.C.3    Goody, R.S.4    Taylor, K.A.5
  • 4
    • 0025783320 scopus 로고
    • Interference with myosin subfragment-1 by site directed mutagenesis of actin
    • Aspenström, P., and R. Karlsson. 1991. Interference with myosin subfragment-1 by site directed mutagenesis of actin. Eur. J. Biochem. 200: 35-41.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 35-41
    • Aspenström, P.1    Karlsson, R.2
  • 6
    • 0028921163 scopus 로고
    • A single myosin head can be cross-linked to the N termini of two adjacent actin monomers
    • Bonafe, N., and P. Chaussepied. 1995. A single myosin head can be cross-linked to the N termini of two adjacent actin monomers. Biophys. J. 68:35s-43s.
    • (1995) Biophys. J. , vol.68
    • Bonafe, N.1    Chaussepied, P.2
  • 8
    • 0024461342 scopus 로고
    • Interaction between stretch of residues 633-642 (actin binding-sites) and nucleotide binding-site on skeletal myosin subfragment-1 heavy-chain
    • Chaussepied, P. 1989. Interaction between stretch of residues 633-642 (actin binding-sites) and nucleotide binding-site on skeletal myosin subfragment-1 heavy-chain. Biochemistry. 28:9123-9128.
    • (1989) Biochemistry , vol.28 , pp. 9123-9128
    • Chaussepied, P.1
  • 9
    • 0342293921 scopus 로고
    • Modifying preselected sites on proteins: The stretch of residues 633-642 of the myosin heavy-chain is part of the actin-binding site
    • Chaussepied, P., and M. F. Morales. 1988. Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy-chain is part of the actin-binding site. Proc. Natl. Acad. Sci. USA. 85:7471-7475.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7471-7475
    • Chaussepied, P.1    Morales, M.F.2
  • 10
    • 0026794025 scopus 로고
    • Removal of the amino-terminal acidic residues of yeast actin. Studies "in vitro" and "in vivo."
    • Cook, R. K., W. T. Blake, and P. A. Rubenstein. 1992. Removal of the amino-terminal acidic residues of yeast actin. Studies "in vitro" and "in vivo." J. Biol. Chem. 267:943-9436.
    • (1992) J. Biol. Chem. , vol.267 , pp. 943-9436
    • Cook, R.K.1    Blake, W.T.2    Rubenstein, P.A.3
  • 12
    • 0026093225 scopus 로고
    • Antibody directed against the 142-148 sequence of the myosin heavy-chain interferes with myosin actin interaction
    • Dan-Moor, M., and A. Muhlrad. 1991. Antibody directed against the 142-148 sequence of the myosin heavy-chain interferes with myosin actin interaction. Biochemistry. 30:400-405.
    • (1991) Biochemistry , vol.30 , pp. 400-405
    • Dan-Moor, M.1    Muhlrad, A.2
  • 14
    • 0024974811 scopus 로고
    • Antibody against the amino terminus of alpha-actin inhibits actomyosin interactions on the presence of ATP
    • Das Gupta, G., and E. Reisler. 1989. Antibody against the amino terminus of alpha-actin inhibits actomyosin interactions on the presence of ATP. J. Mol. Biol. 207:833-836.
    • (1989) J. Mol. Biol. , vol.207 , pp. 833-836
    • Das Gupta, G.1    Reisler, E.2
  • 15
    • 0025938170 scopus 로고
    • Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: Detection of antibodies against the N-terminal segment of actin
    • Das Gupta, G., and E. Reisler. 1991. Nucleotide-induced changes in the interaction of myosin subfragment 1 with actin: detection of antibodies against the N-terminal segment of actin. Biochemistry. 30:9961-9966.
    • (1991) Biochemistry , vol.30 , pp. 9961-9966
    • Das Gupta, G.1    Reisler, E.2
  • 16
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces, and nanometer steps
    • Finer, J. T., R. M. Simmons, and J. A. Spudich. 1994. Single myosin molecule mechanics: piconewton forces, and nanometer steps. Nature. 368:113-118.
    • (1994) Nature , vol.368 , pp. 113-118
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 17
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase-joins on either side of 2 helices close like neighbouring fingers
    • Gerstein, M., G. Schulz, and C. Chothia. 1993. Domain closure in adenylate kinase-joins on either side of 2 helices close like neighbouring fingers. J. Mol. Biol. 229:494-501.
    • (1993) J. Mol. Biol. , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.2    Chothia, C.3
  • 18
    • 0023280069 scopus 로고
    • Calculation of electrostatic potentials in an enzyme active-site
    • Gilson, M. K., and B. H. Honig. 1987. Calculation of electrostatic potentials in an enzyme active-site. Nature. 330:84-86.
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honig, B.H.2
  • 20
    • 0017508185 scopus 로고
    • Active, and rigor muscle stiffness
    • Goldman, Y. E., and R. M. Simmons. 1977. Active, and rigor muscle stiffness. J. Physiol (Lond.). 269:55-57.
    • (1977) J. Physiol (Lond.) , vol.269 , pp. 55-57
    • Goldman, Y.E.1    Simmons, R.M.2
  • 21
    • 0027959756 scopus 로고
    • Structural changes in muscle cross-bridges accompanying force generation
    • Hirose, K., C. Franzini-Armstrong, Y. E. Goldman, and J. M. Murray. 1994. Structural changes in muscle cross-bridges accompanying force generation. J. Cell Biol. 127:763-778.
    • (1994) J. Cell Biol. , vol.127 , pp. 763-778
    • Hirose, K.1    Franzini-Armstrong, C.2    Goldman, Y.E.3    Murray, J.M.4
  • 22
    • 0027291949 scopus 로고
    • Flash, and smash: Rapid freezing of muscle fibres activated by photolysis of caged ATP
    • Hirose, K., T. D. Lennart, J. M. Murray, C. Franzini-Armstrong, and Y. E. Goldman. 1993. Flash, and smash: rapid freezing of muscle fibres activated by photolysis of caged ATP. Biophys. J. 65:397-408.
    • (1993) Biophys. J. , vol.65 , pp. 397-408
    • Hirose, K.1    Lennart, T.D.2    Murray, J.M.3    Franzini-Armstrong, C.4    Goldman, Y.E.5
  • 23
    • 0025153066 scopus 로고
    • Tropomyosin has discrete actin-binding sites with 7-fold, and 14-fold periodicities
    • Hitchcock-DeGregori, S. E., and T. A. Varnell. 1990. Tropomyosin has discrete actin-binding sites with 7-fold, and 14-fold periodicities. J. Mol. Biol. 214:885-896.
    • (1990) J. Mol. Biol. , vol.214 , pp. 885-896
    • Hitchcock-DeGregori, S.E.1    Varnell, T.A.2
  • 24
  • 25
    • 0029016182 scopus 로고
    • Classical electrostatics in biology, and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology, and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 26
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 27
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley, H. E. 1969. The mechanism of muscular contraction. Science. 114:1356-1366.
    • (1969) Science , vol.114 , pp. 1356-1366
    • Huxley, H.E.1
  • 28
    • 0024297340 scopus 로고
    • Three-dimensional structure of the tryptophan synthase α-2-γ-2 multienzyme complex from Salmonella typhimurium
    • Hyde, C. C., S. A. Ahmed, E. A. Padlan, E. W. Miles, and D. R. Davies. 1988. Three-dimensional structure of the tryptophan synthase α-2-γ-2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263:17857-17871.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.C.1    Ahmed, S.A.2    Padlan, E.A.3    Miles, E.W.4    Davies, D.R.5
  • 30
    • 0027522830 scopus 로고
    • Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognised by myosin during ATP-driven sliding motion
    • Johara, M., Y. Y. Toyoshima, A. Ishijima, H. Kojima, T. Yanagida, and K. Sutoh. 1993. Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognised by myosin during ATP-driven sliding motion. Proc. Natl. Acad. Sci. USA. 90:2127-2131.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2127-2131
    • Johara, M.1    Toyoshima, Y.Y.2    Ishijima, A.3    Kojima, H.4    Yanagida, T.5    Sutoh, K.6
  • 32
    • 0022964504 scopus 로고
    • Focusing of electric fields in the active site of Cu-Zn Superoxide dismutase: Effects of ionic strength, and amino-acid modification
    • Klapper, I., R. Hagstrom, R. Fine, K. Sharp, and B. Honig. 1986. Focusing of electric fields in the active site of Cu-Zn Superoxide dismutase: effects of ionic strength, and amino-acid modification. Proteins. 1:47-59.
    • (1986) Proteins , vol.1 , pp. 47-59
    • Klapper, I.1    Hagstrom, R.2    Fine, R.3    Sharp, K.4    Honig, B.5
  • 33
    • 0025937742 scopus 로고
    • Peptide competition of actin activation of myosin subfragment-1 ATPase by an amino terminal actin fragment
    • Kogler, H., A. J. Moir, I. P. Trayer, and J. C. Ruegg. 1991. Peptide competition of actin activation of myosin subfragment-1 ATPase by an amino terminal actin fragment. FEBS Lett. 294:31-34.
    • (1991) FEBS Lett. , vol.294 , pp. 31-34
    • Kogler, H.1    Moir, A.J.2    Trayer, I.P.3    Ruegg, J.C.4
  • 34
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in limus thin filament revealed by 3-dimensional reconstruction
    • 2+-induced tropomyosin movement in limus thin filament revealed by 3-dimensional reconstruction. Nature. 368:65-67.
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 36
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fibre diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., D. Popp, and K. C. Holmes. 1993. Refinement of the F-actin model against X-ray fibre diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 39
    • 0023655060 scopus 로고
    • Anti-actin antibodies: An immunological approach to the myosin actin, and the tropomyosin interfaces
    • Mejean, C., M. Boyer, J. P. Labbe, L. Marlier, Y. Benyamin, and C. Roustan. 1987. Anti-actin antibodies: an immunological approach to the myosin actin, and the tropomyosin interfaces. Biochem. J. 244:571-577.
    • (1987) Biochem. J. , vol.244 , pp. 571-577
    • Mejean, C.1    Boyer, M.2    Labbe, J.P.3    Marlier, L.4    Benyamin, Y.5    Roustan, C.6
  • 40
    • 0023662527 scopus 로고
    • Antibodies directed against N-terminal residues on actin do not block acto-myosin binding
    • Miller, L., M. Kalnoski, Z. Yunossi, J. C. Bulinski, and E. Reisler. 1987. Antibodies directed against N-terminal residues on actin do not block acto-myosin binding. Biochemistry. 26:6064-6070.
    • (1987) Biochemistry , vol.26 , pp. 6064-6070
    • Miller, L.1    Kalnoski, M.2    Yunossi, Z.3    Bulinski, J.C.4    Reisler, E.5
  • 41
    • 0011999851 scopus 로고
    • An induced potential model for myosin head motion along an actin filament in contracting muscle. I. Fundamental muscle properties
    • Mitsui, T., and H. Ohshima. 1993. An induced potential model for myosin head motion along an actin filament in contracting muscle. I. Fundamental muscle properties. Mem. Inst. Sci. Technol. Meiji Univ. 32: 31-62.
    • (1993) Mem. Inst. Sci. Technol. Meiji Univ. , vol.32 , pp. 31-62
    • Mitsui, T.1    Ohshima, H.2
  • 42
    • 0012081861 scopus 로고
    • The interaction of actin with myosin subfragment-1, and with PPDM-cross-linked S1: A H-1-NMR investigation
    • Moir, A. J. G., B. A. Levine, A. J. Goodearl, and I. P. Trayer. 1987. The interaction of actin with myosin subfragment-1, and with PPDM-cross-linked S1: a H-1-NMR investigation. J. Muscle Res. Cell Motil. 8:68-69.
    • (1987) J. Muscle Res. Cell Motil. , vol.8 , pp. 68-69
    • Moir, A.J.G.1    Levine, B.A.2    Goodearl, A.J.3    Trayer, I.P.4
  • 43
    • 0026544877 scopus 로고
    • Structure of the complex between adenylate kinase from escherichiacoli, and the inhibition for AP5A refined at 1.9 Å resolution: A model for a catalytic transition state
    • Muller, C. W., and G. E. Schulz. 1992. Structure of the complex between adenylate kinase from escherichiacoli, and the inhibition for AP5A refined at 1.9 Å resolution: a model for a catalytic transition state. J. Mol. Biol. 224:159-177.
    • (1992) J. Mol. Biol. , vol.224 , pp. 159-177
    • Muller, C.W.1    Schulz, G.E.2
  • 44
    • 0025310575 scopus 로고
    • Refined crystal-structure of the triphosphate conformation of H-ras P21 at 1.35 A resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal-structure of the triphosphate conformation of H-ras P21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351.
    • (1990) EMBO J. , vol.9 , pp. 2351
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 45
    • 0028907268 scopus 로고
    • A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle
    • Piazzessi, G., and V. Lombardi. 1995. A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle. Biophysical J. 68:1966-1979.
    • (1995) Biophysical J. , vol.68 , pp. 1966-1979
    • Piazzessi, G.1    Lombardi, V.2
  • 49
    • 0013850715 scopus 로고
    • Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle
    • Reedy, M. K., K. C. Holmes, and R. T. Tregear. 1965. Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle. Nature. 207:1276-1280.
    • (1965) Nature , vol.207 , pp. 1276-1280
    • Reedy, M.K.1    Holmes, K.C.2    Tregear, R.T.3
  • 50
    • 0022429352 scopus 로고
    • Electrostatic infractions in globular-proteins: Calculations of the pH dependence of the redox potential of cytochrome C551
    • Rogers, N. K., G. R. Moore, and M. J. E. Sternberg. 1985. Electrostatic infractions in globular-proteins: calculations of the pH dependence of the redox potential of cytochrome C551. J. Mol Biol. 182:613-616.
    • (1985) J. Mol Biol. , vol.182 , pp. 613-616
    • Rogers, N.K.1    Moore, G.R.2    Sternberg, M.J.E.3
  • 52
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich, J. A. 1994. How molecular motors work. Nature. 372:515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 53
    • 0023645765 scopus 로고
    • Prediction of electrostatic effects of engineering of protein changes
    • Sternberg, M. J. E., F. R. F. Hayes, A. J. Russell, P. G. Thomas, and A. R. Fersht. 1987. Prediction of electrostatic effects of engineering of protein changes. Nature. 330:86-88.
    • (1987) Nature , vol.330 , pp. 86-88
    • Sternberg, M.J.E.1    Hayes, F.R.F.2    Russell, A.J.3    Thomas, P.G.4    Fersht, A.R.5
  • 54
    • 0025858239 scopus 로고
    • Site-directed mutations of Dictyostelium actin: Disruption of a negative charge cluster at the N terminus
    • Sutoh, K., M. Ando, K. Sutoh, and Y. Y. Tyoshima. 1991. Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N terminus. Proc. Natl Acad Sci. USA. 88:7711-7714.
    • (1991) Proc. Natl Acad Sci. USA , vol.88 , pp. 7711-7714
    • Sutoh, K.1    Ando, M.2    Sutoh, K.3    Tyoshima, Y.Y.4
  • 55
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 Å resolution of the catalytic domains of normal RAS protein, and an oncogenic mutant complexed with GDP
    • Tong, L., A. M. de Vos, M. V. Milburn, and S. H. Kim. 1991. Crystal structures at 2.2 Å resolution of the catalytic domains of normal RAS protein, and an oncogenic mutant complexed with GDP. J. Mol. Biol. 217:503-516.
    • (1991) J. Mol. Biol. , vol.217 , pp. 503-516
    • Tong, L.1    De Vos, A.M.2    Milburn, M.V.3    Kim, S.H.4
  • 56
    • 0026327678 scopus 로고
    • A synthetic peptide of the N-terminus of actin interacts with myosin
    • Van Eyk, J. E., and R. S. Hodges. 1991. A synthetic peptide of the N-terminus of actin interacts with myosin. Biochemistry. 30: 11676-11682.
    • (1991) Biochemistry , vol.30 , pp. 11676-11682
    • Van Eyk, J.E.1    Hodges, R.S.2
  • 57
    • 22944467757 scopus 로고
    • Computer "experiments" on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules
    • Verlet, L. 1967. Computer "experiments" on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules. Physiol. Rev. 159: 98-103.
    • (1967) Physiol. Rev. , vol.159 , pp. 98-103
    • Verlet, L.1
  • 58
    • 0024352016 scopus 로고
    • Binding manner of actin to the Lysine-rich sequence of myosin subfragment-1 in the presence, and absence of ATP
    • Yamamoto, K. 1989. Binding manner of actin to the Lysine-rich sequence of myosin subfragment-1 in the presence, and absence of ATP. Biochemistry. 28:5573-5577.
    • (1989) Biochemistry , vol.28 , pp. 5573-5577
    • Yamamoto, K.1


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