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Volumn 164, Issue 4, 1998, Pages 357-361

Molecular mechanics of two smooth muscle heavy meromyosin constructs that differ by an insert in the motor domain

Author keywords

Actomyosin; Laser trap; Molecular motor; Myosin; Optical trap; Single molecule

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; NUCLEOTIDE;

EID: 0032439710     PISSN: 00016772     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-201X.1998.00451.x     Document Type: Conference Paper
Times cited : (15)

References (31)
  • 1
    • 0027166908 scopus 로고
    • Tissue-specific and developmentally regulated alternative splicing of a visceral isoform of smooth muscle myosin heavy chain
    • Babij, P. 1993. Tissue-specific and developmentally regulated alternative splicing of a visceral isoform of smooth muscle myosin heavy chain. Nucl Acad Res 21, 1467-1471.
    • (1993) Nucl Acad Res , vol.21 , pp. 1467-1471
    • Babij, P.1
  • 2
    • 0029935220 scopus 로고    scopus 로고
    • The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head
    • Bobkov, A.A., Bobkova, E. & Reisler, E. 1996. The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head. Proc Natl Acad Sci USA 93, 2285-2289.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2285-2289
    • Bobkov, A.A.1    Bobkova, E.2    Reisler, E.3
  • 3
    • 0030791973 scopus 로고    scopus 로고
    • Actomyosin interaction in striated muscle
    • Cooke, R. 1997. Actomyosin interaction in striated muscle Physiol. Rev 77, 671-697.
    • (1997) Physiol Rev , vol.77 , pp. 671-697
    • Cooke, R.1
  • 5
    • 0024290415 scopus 로고
    • Two smooth muscle myosin heavy chains differ in their light meromyosin fragment
    • Eddinger, T.J. & Murphy, R.A. 1988. Two smooth muscle myosin heavy chains differ in their light meromyosin fragment. Biochemistry 27, 3807-3811.
    • (1988) Biochemistry , vol.27 , pp. 3807-3811
    • Eddinger, T.J.1    Murphy, R.A.2
  • 6
    • 0023161165 scopus 로고
    • Kinetics of the actomyosin ATPase in muscle fibers
    • Goldman, Y.E. 1987. Kinetics of the actomyosin ATPase in muscle fibers. Annu Rev Physiol 49, 637-654.
    • (1987) Annu Rev Physiol , vol.49 , pp. 637-654
    • Goldman, Y.E.1
  • 7
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap
    • Guilford, W.H., Dupuis, D.E., Kennedy, G., Wu, J., Patlak, J.B. & Warshaw, D.M. 1997. Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap. Biophys J 72, 1006-1021.
    • (1997) Biophys J , vol.72 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 8
    • 0027223768 scopus 로고
    • Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay
    • Harris, D.E. & Warshaw, D.M. 1993. Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay. Circ Res 72, 219-224.
    • (1993) Circ Res , vol.72 , pp. 219-224
    • Harris, D.E.1    Warshaw, D.M.2
  • 9
    • 0013543340 scopus 로고
    • Vascular smooth muscle: Relation between energy metabolism and mechanics
    • Bames CD (ed) Academic Press, New York
    • Hellstrand, P. & Paul, R.J. 1982. Vascular smooth muscle: Relation between energy metabolism and mechanics. In: Bames CD (ed) Vascular smooth muscle: metabolic, ionic and contractile mechanism. pp. 1-35. Academic Press, New York.
    • (1982) Vascular Smooth Muscle: Metabolic, Ionic and Contractile Mechanism , pp. 1-35
    • Hellstrand, P.1    Paul, R.J.2
  • 10
    • 0024421567 scopus 로고
    • Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles
    • Horiuti, K., Somlyo, A.V., Goldman, Y.E. & Somlyo, A.P. 1989. Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles. J Gen Physiol 94, 769-781.
    • (1989) J Gen Physiol , vol.94 , pp. 769-781
    • Horiuti, K.1    Somlyo, A.V.2    Goldman, Y.E.3    Somlyo, A.P.4
  • 11
    • 0026785957 scopus 로고
    • Smooth muscle myosin is composed of homodimeric heavy chains
    • Kelley, C.A., Sellers, J.R., Goldsmith, P.K. & Adelstein, R.S. 1992. Smooth muscle myosin is composed of homodimeric heavy chains. J Biol Chem 267, 2127-2130.
    • (1992) J Biol Chem , vol.267 , pp. 2127-2130
    • Kelley, C.A.1    Sellers, J.R.2    Goldsmith, P.K.3    Adelstein, R.S.4
  • 12
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley, C.A., Takahashi, M., Yu, J.H. & Adelstein, R.S. 1993. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J Biol Chem 268, 12848-12854.
    • (1993) J Biol Chem , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 13
    • 0029930738 scopus 로고    scopus 로고
    • Nucleotide binding by actomyosin as a determinant of relaxation kinetics of rabbit phasic and tonic smooth muscle
    • Khromov, A.S., Somlyo, A.V. & Somlyo, A.P. 1996. Nucleotide binding by actomyosin as a determinant of relaxation kinetics of rabbit phasic and tonic smooth muscle. J Physiol 492, 669-673.
    • (1996) J Physiol , vol.492 , pp. 669-673
    • Khromov, A.S.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 14
    • 0025817957 scopus 로고
    • Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle
    • Malmqvist, U. & Arner, A. 1991. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Pflugers Arch 418, 523-530.
    • (1991) Pflugers Arch , vol.418 , pp. 523-530
    • Malmqvist, U.1    Arner, A.2
  • 15
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • Marston, S.B. & Taylor, R.W. 1980. Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles. J Mol Biol 139, 573-600.
    • (1980) J Mol Biol , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, R.W.2
  • 16
    • 0030909101 scopus 로고    scopus 로고
    • Myosin isoforms and functional diversity in vertebrate smooth muscle
    • Murphy, R.A., Walker, J.S. & Strauss, J.D. 1997. Myosin isoforms and functional diversity in vertebrate smooth muscle. Comp Biochem Physiol 117B, 51-60.
    • (1997) Comp Biochem Physiol , vol.117 B , pp. 51-60
    • Murphy, R.A.1    Walker, J.S.2    Strauss, J.D.3
  • 17
    • 0024370066 scopus 로고
    • Identification of two types of smooth muscle myosin heavy chain isoforms by cDNA cloning and immunoblot analysis
    • Nagai, R., Kuro-O., M. Babij, P. & Periasamy, M. 1989. Identification of two types of smooth muscle myosin heavy chain isoforms by cDNA cloning and immunoblot analysis. J Biol Chem 264, 9734-9737.
    • (1989) J Biol Chem , vol.264 , pp. 9734-9737
    • Nagai, R.1    Kuro-O, M.2    Babij, P.3    Periasamy, M.4
  • 18
    • 0027194750 scopus 로고
    • Measuring kinetics of complex single ion channel data using mean-variance histograms
    • Patlak, J.B. 1993. Measuring kinetics of complex single ion channel data using mean-variance histograms. Biophys J 65, 29-42.
    • (1993) Biophys J , vol.65 , pp. 29-42
    • Patlak, J.B.1
  • 19
    • 0029909606 scopus 로고    scopus 로고
    • Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins
    • Perreault-Micale, C.L., Kalabokis, V.N., Nyitray, L. & Szent Gyorgyi, A.G. 1996. Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins. J Mus Res Cell Motil 17, 543-553.
    • (1996) J Mus Res Cell Motil , vol.17 , pp. 543-553
    • Perreault-Micale, C.L.1    Kalabokis, V.N.2    Nyitray, L.3    Szent Gyorgyi, A.G.4
  • 20
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment, I., Rypniewski, W.R., Schmidt-Base, K. et al. 1993. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-65.
    • (1993) Science , vol.261 , pp. 50-65
    • Rayment, I.1    Rypniewski, W.R.2    Schmidt-Base, K.3
  • 21
    • 0029561337 scopus 로고
    • Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin
    • Rovner, A.S., Freyzon, Y. & Trybus, K.M. 1995. Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J Biol Chem 270, 30260-30263.
    • (1995) J Biol Chem , vol.270 , pp. 30260-30263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 22
    • 0031031962 scopus 로고    scopus 로고
    • An insert in the motor domain determines the functional properties of expressed smooth muscle myoisn isoforms
    • Rovner, A.S., Freyzon, Y. & Trybus, K.M. 1997. An insert in the motor domain determines the functional properties of expressed smooth muscle myoisn isoforms. J Musc Res Cell Motil 18, 103-110.
    • (1997) J Musc Res Cell Motil , vol.18 , pp. 103-110
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 23
    • 0027724301 scopus 로고
    • Myosin isoforms in smooth muscle: How may they affect function and structure?
    • Somlyo, A.P. 1993. Myosin isoforms in smooth muscle: how may they affect function and structure? J Mus Res Cell Motil 14, 557-563.
    • (1993) J Mus Res Cell Motil , vol.14 , pp. 557-563
    • Somlyo, A.P.1
  • 24
    • 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
  • 25
    • 0032513032 scopus 로고    scopus 로고
    • Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket
    • Sweeney, H.L., Rosenfeld, S.S., Brown, F. et al., 1998. Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket. J Biol Chem 273, 6262-6270.
    • (1998) J Biol Chem , vol.273 , pp. 6262-6270
    • Sweeney, H.L.1    Rosenfeld, S.S.2    Brown, F.3
  • 26
    • 0024811666 scopus 로고
    • Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin
    • Trybus, K.M. & Henry, L. 1989. Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin. J Cell Biol 109, 2879-2886.
    • (1989) J Cell Biol , vol.109 , pp. 2879-2886
    • Trybus, K.M.1    Henry, L.2
  • 27
    • 0027252626 scopus 로고
    • Smooth muscle myosin heavy chains combine to form three native myosin isoforms
    • Tsao, A.E. & Eddinger, T.J. 1993. Smooth muscle myosin heavy chains combine to form three native myosin isoforms. Am J Physiol 264, H1653-H1662.
    • (1993) Am J Physiol , vol.264
    • Tsao, A.E.1    Eddinger, T.J.2
  • 28
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda, T.Q.P., Ruppel, K.M. & Spudich, J.A. 1994. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature 368, 567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 29
    • 0019400605 scopus 로고
    • Actin typing on total cellular extracts
    • Vandekerckhove, J. & Weber, K. 1981. Actin typing on total cellular extracts. Eur J Biochem 113, 595-603.
    • (1981) Eur J Biochem , vol.113 , pp. 595-603
    • Vandekerckhove, J.1    Weber, K.2
  • 30
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw, D.M., Desrosiers, J.M., Work, S.S. & Trybus, K.M. 1990. Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J Cell Biol 111, 453-463.
    • (1990) J Cell Biol , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4
  • 31
    • 0027223294 scopus 로고
    • Identification of a novel smooth muscle myosin heavy chain cDNA: Isoform diversity in the S1 head region
    • White, S., Martin, A.F. & Periasamy, M. 1993. Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head region. Am J Physiol 264, C1252-C1258.
    • (1993) Am J Physiol , vol.264
    • White, S.1    Martin, A.F.2    Periasamy, M.3


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