메뉴 건너뛰기




Volumn 3, Issue 9, 1996, Pages 796-802

ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; MYOSIN; MYOSIN SUBFRAGMENT 1;

EID: 0029745362     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0996-796     Document Type: Article
Times cited : (76)

References (40)
  • 1
    • 0022462908 scopus 로고    scopus 로고
    • The mechanism of muscle contraction
    • Cooke, R. The mechanism of muscle contraction. Critical Reviews in Biochemistry 21, 53-118 (1996).
    • (1996) Critical Reviews in Biochemistry , vol.21 , pp. 53-118
    • Cooke, R.1
  • 2
    • 0023161165 scopus 로고
    • Kinetics of the actomyosin ATPase in muscle fibers
    • Goldman, Y.E. Kinetics of the actomyosin ATPase in muscle fibers. Ann. Rev. Physiol. 49, 637-654 (1987).
    • (1987) Ann. Rev. Physiol. , vol.49 , pp. 637-654
    • Goldman, Y.E.1
  • 4
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment, I. et al. Three-dimensional structure of myosin subfragment-1: A molecular motor. Science 261, 50-57 (1993).
    • (1993) Science , vol.261 , pp. 50-57
    • Rayment, I.1
  • 5
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., Popp, D. & Holmes, K.C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826-836 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 7
    • 0027220271 scopus 로고
    • Three dimensional atomic model of F-actin decorated with Dictyostelium myosin S1
    • Schroder, R.R. et al. Three dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature 364, 171-174 (1993).
    • (1993) Nature , vol.364 , pp. 171-174
    • Schroder, R.R.1
  • 8
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I. et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-65 (1993).
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1
  • 9
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to cross-bridges in contracting muscle fibers
    • Cooke, R., Crowder, M.S. & Thomas, D.D. Orientation of spin labels attached to cross-bridges in contracting muscle fibers. Nature 30, 776-778 (1982).
    • (1982) Nature , vol.30 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 10
    • 0026513108 scopus 로고
    • Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibers
    • Tanner, J.W., Thomas, D.W. & Goldman, Y.E. Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibers. J. Mol. Biol. 223, 185-203 (1992).
    • (1992) J. Mol. Biol. , vol.223 , pp. 185-203
    • Tanner, J.W.1    Thomas, D.W.2    Goldman, Y.E.3
  • 11
    • 0028962794 scopus 로고
    • Orientational dynamics of indane dione spin-labeled myosin heads in relaxed and contracting skeletal muscle fibers
    • Roopnarine, O. & Thomas, D.D. Orientational dynamics of indane dione spin-labeled myosin heads in relaxed and contracting skeletal muscle fibers, Biophys. J. 68, 1461-1471 (1995).
    • (1995) Biophys. J. , vol.68 , pp. 1461-1471
    • Roopnarine, O.1    Thomas, D.D.2
  • 12
    • 0021985525 scopus 로고
    • Angle of active site of myosin heads in contracting muscle during sudden length changes
    • Yanagida, T. Angle of active site of myosin heads in contracting muscle during sudden length changes. J. Mus. Res. Cell Motility 6, 43-52 (1985).
    • (1985) J. Mus. Res. Cell Motility , vol.6 , pp. 43-52
    • Yanagida, T.1
  • 13
    • 0029080466 scopus 로고
    • The myosin catalytic domain does not rotate during the working power stroke
    • Zhao, L, Pate, E., Baker, A.J. & Cooke, R. The myosin catalytic domain does not rotate during the working power stroke. Biophys. J. 69, 994-999 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 994-999
    • Zhao, L.1    Pate, E.2    Baker, A.J.3    Cooke, R.4
  • 14
    • 0027934341 scopus 로고
    • Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length
    • Trybus, K.M. Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length. J. Biol. Chem. 269, 20819-20822 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 20819-20822
    • Trybus, K.M.1
  • 15
    • 0027426228 scopus 로고
    • Skeletal muscle myosin light chains are essential for physiological speeds of shortening
    • Lowey, S, Waller, G.S. & Trybus, K.M. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature 365, 454-456 (1993).
    • (1993) Nature , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 16
    • 0029176506 scopus 로고
    • A 35-angstrom movement of smooth muscle myosin on ADP release
    • Whittaker, M. et al. A 35-angstrom movement of smooth muscle myosin on ADP release. Nature 378, 748-751 (1995).
    • (1995) Nature , vol.378 , pp. 748-751
    • Whittaker, M.1
  • 17
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda, T.Q.P., Abramson, P.D. & Spudich, J.A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl. Acad. Sci. USA 93, 4459-4464 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.P.1    Abramson, P.D.2    Spudich, J.A.3
  • 18
    • 0029057460 scopus 로고
    • Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle
    • Irving, M. et al. Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature 375, 688-691 (1995).
    • (1995) Nature , vol.375 , pp. 688-691
    • Irving, M.1
  • 19
    • 0029562245 scopus 로고
    • A 32-degrees tail swing in brush border myosin I on Adp release
    • Jontes, J.D., Wilson-Kubalek, E.M. & Milligan, R.A. A 32-degrees tail swing in brush border myosin I on Adp release. Nature 378, 751-753 (1995).
    • (1995) Nature , vol.378 , pp. 751-753
    • Jontes, J.D.1    Wilson-Kubalek, E.M.2    Milligan, R.A.3
  • 20
    • 0023161168 scopus 로고
    • Spectroscopic probes of muscle cross-bridge rotation
    • Thomas, D.D. Spectroscopic probes of muscle cross-bridge rotation. Annu. Rev. Physiol. 46, 691-709 (1987).
    • (1987) Annu. Rev. Physiol. , vol.46 , pp. 691-709
    • Thomas, D.D.1
  • 21
    • 0019193255 scopus 로고
    • Orientation of spin-labeled myosin heads in glycerinated muscle fibers
    • Thomas, D.D. & Cooke, R. Orientation of spin-labeled myosin heads in glycerinated muscle fibers. Biophys. J. 32, 891-906 (1980).
    • (1980) Biophys. J. , vol.32 , pp. 891-906
    • Thomas, D.D.1    Cooke, R.2
  • 22
    • 0022618554 scopus 로고
    • High-resolution detection of muscle crossbridge orientation by electron paramagnetic resonance
    • Barnett, V.A., Fajer, P., Polnaszek, C.F. & Thomas, D.D. High-resolution detection of muscle crossbridge orientation by electron paramagnetic resonance. Biophys. J. 49, 144-146 (1986).
    • (1986) Biophys. J. , vol.49 , pp. 144-146
    • Barnett, V.A.1    Fajer, P.2    Polnaszek, C.F.3    Thomas, D.D.4
  • 23
    • 0029863187 scopus 로고    scopus 로고
    • Fluorescent probes of the orientation of myosin regulatory tight chains in relaxed, rigor, and contracting muscle
    • Ling, N., Shrimpton, C., Sleep, J, Kendrick-Jones, J. & Irving, M. Fluorescent probes of the orientation of myosin regulatory tight chains in relaxed, rigor, and contracting muscle. Biophys. J. 70, 1836-1846 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1836-1846
    • Ling, N.1    Shrimpton, C.2    Sleep, J.3    Kendrick-Jones, J.4    Irving, M.5
  • 24
    • 0028987918 scopus 로고
    • The creatine kinase equilibrium, free [Adp] and myosin atpase in vascular smooth muscle cross-bridges
    • Clark, J.F., Kemp, G.J. & Radda, G.K. The creatine kinase equilibrium, free [Adp] and myosin atpase in vascular smooth muscle cross-bridges, J. Theoretical Biol. 173, 207-211 (1995).
    • (1995) J. Theoretical Biol. , vol.173 , pp. 207-211
    • Clark, J.F.1    Kemp, G.J.2    Radda, G.K.3
  • 25
    • 0027408994 scopus 로고
    • The effects of MgADP on cross-bridge kinetics: A laser flash photolysis study of guinea-pig smooth muscle
    • Nishiye, E., Somlyo, A.V, Torok, K. & Somlyo, A.P. The effects of MgADP on cross-bridge kinetics: a laser flash photolysis study of guinea-pig smooth muscle. J. Physiol. 460, 247-71 (1993).
    • (1993) J. Physiol. , vol.460 , pp. 247-271
    • Nishiye, E.1    Somlyo, A.V.2    Torok, K.3    Somlyo, A.P.4
  • 26
    • 0027787986 scopus 로고
    • Flash photolysis studies of relaxation and cross-bridge detachment: Higher sensitivity of tonic than phasic smooth muscle to MgADP
    • Fuglsang, A., Khromov, A., Torok, K., Somlyo, A.V. & Somlyo, A.P. Flash photolysis studies of relaxation and cross-bridge detachment: higher sensitivity of tonic than phasic smooth muscle to MgADP. J. Musc. Res. Cell Motility 14, 666-677 (1993).
    • (1993) J. Musc. Res. Cell Motility , vol.14 , pp. 666-677
    • Fuglsang, A.1    Khromov, A.2    Torok, K.3    Somlyo, A.V.4    Somlyo, A.P.5
  • 27
    • 0023664088 scopus 로고
    • Effect of phosphorylation on the binding of smooth mscle heavy meromyosin X ADP to actin
    • Greene, LE. & Sellers, J.R. Effect of phosphorylation on the binding of smooth mscle heavy meromyosin X ADP to actin. J. Biol. Chem. 262, 4177-4181 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 4177-4181
    • Greene, L.E.1    Sellers, J.R.2
  • 29
    • 0026082863 scopus 로고
    • The dynamics of actin and myosin association and the crossbridge model of muscle contraction
    • Geeves, M.A. The dynamics of actin and myosin association and the crossbridge model of muscle contraction, Biochem. J. 274 1-14 (1991).
    • (1991) Biochem. J. , vol.274 , pp. 1-14
    • Geeves, M.A.1
  • 30
    • 0029975892 scopus 로고    scopus 로고
    • Orientation changes in myosin regulatory light chains following photorelease of atp in skinned musclefibers
    • Allen, T.S., Ling, N., Irving, M. & Goldman, YE. Orientation changes in myosin regulatory light chains following photorelease of atp in skinned musclefibers. Biophys. J. 70, 1847-1862 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1847-1862
    • Allen, T.S.1    Ling, N.2    Irving, M.3    Goldman, Y.E.4
  • 31
    • 0026619792 scopus 로고
    • Paramagnetic probes attached to a light chain on the myosin head are highly disordered in active muscle fibers
    • Hambly, B., Franks, K. & Cooke, R. Paramagnetic probes attached to a light chain on the myosin head are highly disordered in active muscle fibers. Biophys. J. 63, 306-313 (1992).
    • (1992) Biophys. J. , vol.63 , pp. 306-313
    • Hambly, B.1    Franks, K.2    Cooke, R.3
  • 32
    • 0022270772 scopus 로고
    • Effects of Ca2+ on the conformation and enzymatic activity of smooth muscle myosin
    • Ikebe, M. & Hartshorne, D.J. Effects of Ca2+ on the conformation and enzymatic activity of smooth muscle myosin. J. Biol. Chem. 260, 13146-13153 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 13146-13153
    • Ikebe, M.1    Hartshorne, D.J.2
  • 33
    • 0026924047 scopus 로고
    • A new method to specifically label thiophosphorylatable proteins with extrinsic probes. Labeling of serine-19 of the regulatory light chain of smooth muscle myosin
    • Facemyer, K.C. & Cremo, C.R. A new method to specifically label thiophosphorylatable proteins with extrinsic probes. Labeling of serine-19 of the regulatory light chain of smooth muscle myosin. Bioconjugate Chem. 3, 408-413 (1992).
    • (1992) Bioconjugate Chem. , vol.3 , pp. 408-413
    • Facemyer, K.C.1    Cremo, C.R.2
  • 34
    • 0028918058 scopus 로고
    • Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin
    • Cremo, C.R., Sellers, J.R. & Facemyer, K.C. Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin. J. Biol. Chem. 270, 2171-2175 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2171-2175
    • Cremo, C.R.1    Sellers, J.R.2    Facemyer, K.C.3
  • 35
    • 0021824642 scopus 로고
    • Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: Preparation of heavy meromyosin and subfragment 1 with intact 20 000-dalton light chains
    • Ikebe, M. & Hartshorne, D.J. Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: preparation of heavy meromyosin and subfragment 1 with intact 20 000-dalton light chains. Biochemistry 24, 2380-2387 (1985).
    • (1985) Biochemistry , vol.24 , pp. 2380-2387
    • Ikebe, M.1    Hartshorne, D.J.2
  • 36
    • 0015511484 scopus 로고
    • A new method for producing myosin subfragment-1
    • Cooke, R. A new method for producing myosin subfragment-1. Biochem. Biophys. Res. Commun. 49, 1021-1028 (1972).
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 1021-1028
    • Cooke, R.1
  • 37
    • 0026052346 scopus 로고
    • Exchange of the fluorescence-labeled 20,000-Dalton light chain of smooth muscle myosin
    • Morita, J.-I., Takashi, R. & Ikebe, M. Exchange of the fluorescence-labeled 20,000-Dalton light chain of smooth muscle myosin. Biochemistry, 30 9539-9545 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9539-9545
    • Morita, J.-I.1    Takashi, R.2    Ikebe, M.3
  • 38
    • 0027419741 scopus 로고
    • Chimeric regulatory light chains as probes of smooth muscle myosin
    • Trybus, K.M. & Chatman, T.A. Chimeric regulatory light chains as probes of smooth muscle myosin. J. Biol. Chem. 268, 4412-4419 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4412-4419
    • Trybus, K.M.1    Chatman, T.A.2
  • 39
    • 0001688597 scopus 로고
    • Estimating slow-motional rotational correlation times for nitroxides by electron spin resonance
    • Goldman, S.A., Bruno, G.V. & Freed, J.H. Estimating slow-motional rotational correlation times for nitroxides by electron spin resonance. J. Phys. Chem. 76, 1858-1860 (1972).
    • (1972) J. Phys. Chem. , vol.76 , pp. 1858-1860
    • Goldman, S.A.1    Bruno, G.V.2    Freed, J.H.3
  • 40
    • 0001250693 scopus 로고
    • General method for multiparameter fitting of high-resolution EPR spectra using a simplex algorithm
    • Fajer, P.G, Bennett, R.L.H., Polnaszek, C.F., Fajer, E.A & Thomas, D.D. General method for multiparameter fitting of high-resolution EPR spectra using a simplex algorithm. J. Mag. Res. 88, 111-125 (1990).
    • (1990) J. Mag. Res. , vol.88 , pp. 111-125
    • Fajer, P.G.1    Bennett, R.L.H.2    Polnaszek, C.F.3    Fajer, E.A.4    Thomas, D.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.