메뉴 건너뛰기




Volumn 19, Issue 5, 1998, Pages 491-504

ATPase kinetics of the Dictyostelium discoideum myosin II motor domain

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE DERIVATIVE; MYOSIN;

EID: 0031872841     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005304408812     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 0021923806 scopus 로고
    • Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments
    • ANDO, T. & SCALES, D. (1985) Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments. J. Biol. Chem. 260, 2321-7.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2321-2327
    • Ando, T.1    Scales, D.2
  • 2
    • 0027448578 scopus 로고
    • Two different rigor complexes of myosin subfragment 1 and actin
    • ANDREEV, O. A., ANDREEVA, A. L., MARKIN, V. S. & BOREJDO, J. (1993) Two different rigor complexes of myosin subfragment 1 and actin. Biochemistry 32, 12046-53.
    • (1993) Biochemistry , vol.32 , pp. 12046-12053
    • Andreev, O.A.1    Andreeva, A.L.2    Markin, V.S.3    Borejdo, J.4
  • 5
    • 0015846921 scopus 로고
    • The reversibility of adenosine triphosphate cleavage by myosin
    • BAGSHAW, C. R. & TRENTHAM, D. R. (1973) The reversibility of adenosine triphosphate cleavage by myosin. Biochem. J. 133, 323-8.
    • (1973) Biochem. J. , vol.133 , pp. 323-328
    • Bagshaw, C.R.1    Trentham, D.R.2
  • 6
    • 0016233229 scopus 로고
    • 2+-dependent adenosine triphosphatase reaction
    • 2+-dependent adenosine triphosphatase reaction. Biochem. J. 141, 331-49.
    • (1974) Biochem. J. , vol.141 , pp. 331-349
    • Bagshaw, C.R.1    Trentham, D.R.2
  • 8
    • 0025344156 scopus 로고
    • A continuous fluorimetric assay for ATPase activity
    • BANIK, U. & ROY, S. (1990) A continuous fluorimetric assay for ATPase activity. Biochem. J. 266, 611-4.
    • (1990) Biochem. J. , vol.266 , pp. 611-614
    • Banik, U.1    Roy, S.2
  • 9
    • 0031555481 scopus 로고    scopus 로고
    • X-ray crystal structure and solution fluorescence characterization of Mg.2′(3′)-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain
    • BAUER, C. B., KUHLMAN, P. A., BAGSHAW C. R. & RAYMENT, I. (1997) X-ray crystal structure and solution fluorescence characterization of Mg.2′(3′)-O-(N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain. J. Mol. Biol. 274, 394-407.
    • (1997) J. Mol. Biol. , vol.274 , pp. 394-407
    • Bauer, C.B.1    Kuhlman, P.A.2    Bagshaw, C.R.3    Rayment, I.4
  • 10
    • 0029892859 scopus 로고    scopus 로고
    • Kinetics of association of myosin subfragment 1 to unlabeled and pyrenyl-labeled actin
    • BLANCHOIN, L., DIDRY, D., CARLIER, M. F. & PANTOLINI, D. (1996) Kinetics of association of myosin subfragment 1 to unlabeled and pyrenyl-labeled actin. J. Biol. Chem. 271, 12380-86.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12380-12386
    • Blanchoin, L.1    Didry, D.2    Carlier, M.F.3    Pantolini, D.4
  • 11
    • 0030761390 scopus 로고    scopus 로고
    • Nucleotide and actin binding properties of the isolated motor domain from Dictyostelium discoideum myosin
    • BOBKOV, A. A., SUTOH, K. & REISLER, E. (1997) Nucleotide and actin binding properties of the isolated motor domain from Dictyostelium discoideum myosin. J. Muscle Res. Cell Motil. 18, 563-71.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 563-571
    • Bobkov, A.A.1    Sutoh, K.2    Reisler, E.3
  • 12
    • 0030045748 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of fluorescent ribose-modified ATP analogs upon interaction with skeletal muscle myosin subfragment 1
    • CONIBEAR, P. B., JEFFREYS, D. S., SEEHRA, C. K., EATON, R. J. & BAGSHAW, C. R. (1996) Kinetic and spectroscopic characterization of fluorescent ribose-modified ATP analogs upon interaction with skeletal muscle myosin subfragment 1. Biochemistry 35, 2299-2308.
    • (1996) Biochemistry , vol.35 , pp. 2299-2308
    • Conibear, P.B.1    Jeffreys, D.S.2    Seehra, C.K.3    Eaton, R.J.4    Bagshaw, C.R.5
  • 13
    • 14444269011 scopus 로고    scopus 로고
    • Measurement of ATPase activities of myosin at the level of tracks and single molecules
    • (edited by SUGI, H. & POLLACK, G.). New York: Plenum Press, in press
    • CONIBEAR, P. B., KUHLMAN, P. A. & BAGSHAW, C. R. (1998) Measurement of ATPase activities of myosin at the level of tracks and single molecules. In Mechanism of Work Production and Work Absorption in Muscle (edited by SUGI, H. & POLLACK, G.). New York: Plenum Press, in press.
    • (1998) Mechanism of Work Production and Work Absorption in Muscle
    • Conibear, P.B.1    Kuhlman, P.A.2    Bagshaw, C.R.3
  • 15
    • 0011364439 scopus 로고
    • Structural studies of myosin:nucleotide complexes: A revised model for the molecular basis of muscle contraction
    • FISHER, A. J., SMITH, C. A., THODEN, J., SMITH, R., SUTOH, K., HOLDEN, H. M. & RAYMENT, I. (1995a) Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys. J. 68, 19s-28s.
    • (1995) Biophys. J. , vol.68
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.3    Smith, R.4    Sutoh, K.5    Holden, H.M.6    Rayment, I.7
  • 17
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • FUNATSU, T., HARADA, Y., TOKUNAGA, M., SAITO, K. & YANAGIDA, T. (1995) Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374, 555-9.
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 18
    • 0026082863 scopus 로고
    • The dynamics of actin and myosin association and the crossbridge model of muscle contraction
    • GEEVES, M. A. (1991) The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem. J. 274, 1-14.
    • (1991) Biochem. J. , vol.274 , pp. 1-14
    • Geeves, M.A.1
  • 19
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • HIRATSUKA, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 20
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever arm hypothesis of muscle contraction
    • HOLMES, K. C. (1997) The swinging lever arm hypothesis of muscle contraction. Curr. Biol. 7, R112-8.
    • (1997) Curr. Biol. , vol.7
    • Holmes, K.C.1
  • 22
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerisation and on binding of heavy meromyosin
    • KOUYAMA, T. & MIHASHI, K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerisation and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-8.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 23
    • 0039448598 scopus 로고    scopus 로고
    • Characterisation of the crystallised myosin motor domain derived from Dictyostelium
    • KUHLMAN, P. A. & BAGSHAW, C. R. (1996) Characterisation of the crystallised myosin motor domain derived from Dictyostelium. Molecular Biology of the Cell 7, 196a.
    • (1996) Molecular Biology of the Cell , vol.7
    • Kuhlman, P.A.1    Bagshaw, C.R.2
  • 24
    • 0030472486 scopus 로고    scopus 로고
    • A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using μg quantities of protein
    • KURZAWA, S. E. & GEEVES, M. A. (1996) A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using μg quantities of protein. J. Muscle Res. Cell Motil. 17, 669-76.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 669-676
    • Kurzawa, S.E.1    Geeves, M.A.2
  • 25
    • 0031028517 scopus 로고    scopus 로고
    • Dictyostelium discoideum myosin II: Characterisation of functional myosin motor fragments
    • KURZAWA, S. E., MANSTEIN, D. J. & GEEVES, M. A. (1997) Dictyostelium discoideum myosin II: characterisation of functional myosin motor fragments. Biochemistry 36, 317-23.
    • (1997) Biochemistry , vol.36 , pp. 317-323
    • Kurzawa, S.E.1    Manstein, D.J.2    Geeves, M.A.3
  • 26
    • 0024960744 scopus 로고
    • Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum
    • MANSTEIN, D. J., KUPPEL, K. M. & SPUDICH, J. A. (1989) Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum. Science 246, 656-8.
    • (1989) Science , vol.246 , pp. 656-658
    • Manstein, D.J.1    Kuppel, K.M.2    Spudich, J.A.3
  • 27
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • MARGOSSIAN, S. S. & LOWEY, S. (1982) Preparation of myosin and its subfragments from rabbit skeletal muscle. Meth. Enzymol. 85, 55-71.
    • (1982) Meth. Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 28
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • PARDEE, J. D. & SPUDICH, J. A. (1982) Purification of muscle actin. Meth. Enzymol. 85, 164-81.
    • (1982) Meth. Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 30
    • 0026349335 scopus 로고
    • Is there a rate-limiting step before GTP cleavage by H-ras p21?
    • RENSLAND, H., LAUTWEIN, A., WITTINGHOFER, A. & GOODY, R. S. (1991) Is there a rate-limiting step before GTP cleavage by H-ras p21? Biochemistry 30, 11181-5.
    • (1991) Biochemistry , vol.30 , pp. 11181-11185
    • Rensland, H.1    Lautwein, A.2    Wittinghofer, A.3    Goody, R.S.4
  • 31
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
    • RIGLER, R., METS, U., WIDENGREN, J. & KASK, P. (1993) Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur. Biophys. J. 22, 169-75.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widengren, J.3    Kask, P.4
  • 32
    • 0027267667 scopus 로고
    • Kinetics characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum
    • RITCHIE, M. D., GEEVES, M. A., WOODWARD, S. K. & MANSTEIN, D. J. (1993) Kinetics characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum. Proc. Nat Acad. Sci. USA 90, 8619-23.
    • (1993) Proc. Nat Acad. Sci. USA , vol.90 , pp. 8619-8623
    • Ritchie, M.D.1    Geeves, M.A.2    Woodward, S.K.3    Manstein, D.J.4
  • 33
    • 0029731663 scopus 로고    scopus 로고
    • Structure-function analysis of the motor domain of myosin
    • RUPPEL, K. M. & SPUDICH, J. A. (1996) Structure-function analysis of the motor domain of myosin. Ann. Rev. Cell Dev. Biol. 12, 543-73.
    • (1996) Ann. Rev. Cell Dev. Biol. , vol.12 , pp. 543-573
    • Ruppel, K.M.1    Spudich, J.A.2
  • 34
    • 0030664537 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II
    • SHIMADA, T., SASAKI, N., OHKURA, R. & SUTOH, K. (1997) Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum myosin II. Biochemistry 36, 14037-43.
    • (1997) Biochemistry , vol.36 , pp. 14037-14043
    • Shimada, T.1    Sasaki, N.2    Ohkura, R.3    Sutoh, K.4
  • 35
    • 0021368686 scopus 로고
    • Kinetics of the interaction between actin, ADP and cardiac myosin-S1
    • SIEMANKOWSKI, R. F. & WHITE, H. D. (1984) Kinetics of the interaction between actin, ADP and cardiac myosin-S1. J. Biol. Chem. 259, 5045-53.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5045-5053
    • Siemankowski, R.F.1    White, H.D.2
  • 36
    • 0029161763 scopus 로고
    • X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 Å resolution
    • SMITH, C. A. & RAYMENT, I. (1995) X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 Å resolution. Biochemistry 34, 8973-81.
    • (1995) Biochemistry , vol.34 , pp. 8973-8981
    • Smith, C.A.1    Rayment, I.2
  • 37
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • SMITH, C. A. & RAYMENT, I. (1996) X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35, 5404-17.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 38
    • 0018368483 scopus 로고
    • Mechanism of actomyosin ATPase and the problem of muscle contraction
    • TAYLOR, E. W. (1979) Mechanism of actomyosin ATPase and the problem of muscle contraction. CRC Crit. Rev. Biochem. 6, 103-64.
    • (1979) CRC Crit. Rev. Biochem. , vol.6 , pp. 103-164
    • Taylor, E.W.1
  • 40
    • 0023265887 scopus 로고
    • Kinetics of actin elongation and depolymerization at the pointed end
    • WEBER, A., NORTHROP, J., BISHOP, M. F., FERRONE, F. A. & MOOSEKER, M. S. (1987) Kinetics of actin elongation and depolymerization at the pointed end. Biochemistry 26, 2528-36.
    • (1987) Biochemistry , vol.26 , pp. 2528-2536
    • Weber, A.1    Northrop, J.2    Bishop, M.F.3    Ferrone, F.A.4    Mooseker, M.S.5
  • 41
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • WEEDS, A. G. & TAYLOR, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 257, 54-6.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 42
    • 0022429887 scopus 로고
    • Calcium regulation of molluscan myosin ATPase in the absence of actin
    • WELLS, C. & BAGSHAW, C. R. (1985) Calcium regulation of molluscan myosin ATPase in the absence of actin. Nature 313, 696-7.
    • (1985) Nature , vol.313 , pp. 696-697
    • Wells, C.1    Bagshaw, C.R.2
  • 43
    • 0026018966 scopus 로고
    • Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl) ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two acto-S1.ADP complexes
    • WOODWARD, S. K., ECCLESTON, J. F. & GEEVES, M. A. (1991) Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl) ATP with myosin subfragment 1 and actomyosin subfragment 1: characterization of two acto-S1.ADP complexes. Biochemistry 30, 422-30.
    • (1991) Biochemistry , vol.30 , pp. 422-430
    • Woodward, S.K.1    Eccleston, J.F.2    Geeves, M.A.3
  • 44
    • 0028785981 scopus 로고
    • Kinetic characterization of the catalytic domain of Dictyostelium discoideum myosin
    • WOODWARD, S. K. A., GEEVES, M. A. & MANSTEIN, D. J. (1995) Kinetic characterization of the catalytic domain of Dictyostelium discoideum myosin. Biochemistry 34, 16056-64.
    • (1995) Biochemistry , vol.34 , pp. 16056-16064
    • Woodward, S.K.A.1    Geeves, M.A.2    Manstein, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.