메뉴 건너뛰기




Volumn 76, Issue 2, 1999, Pages 985-992

Cooperativity between two heads of Dictyostelium myosin II in in vitro motility and ATP hydrolysis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); ADENOSINE TRIPHOSPHATE; MYOSIN; NICKEL;

EID: 0033037675     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77262-0     Document Type: Article
Times cited : (30)

References (46)
  • 3
    • 0028899953 scopus 로고
    • Failure of a single-headed kinesin to track parallel to microtubule protofilaments
    • Berliner, E., E. C. Young, K. Anderson, H. K. Mahtani, and J. Gelles. 1995. Failure of a single-headed kinesin to track parallel to microtubule protofilaments. Nature. 373:718-721.
    • (1995) Nature , vol.373 , pp. 718-721
    • Berliner, E.1    Young, E.C.2    Anderson, K.3    Mahtani, H.K.4    Gelles, J.5
  • 4
    • 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., E. A. Bobkova, S. H. Lin, and E. Reisler. 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.A.2    Lin, S.H.3    Reisler, E.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0017873220 scopus 로고
    • Generation of force by single-headed myosin
    • Cooke, R., and K. E. Franks. 1978. Generation of force by single-headed myosin. J. Mol. Biol. 120:361-373.
    • (1978) J. Mol. Biol. , vol.120 , pp. 361-373
    • Cooke, R.1    Franks, K.E.2
  • 9
    • 0028918058 scopus 로고
    • Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin
    • Cremo, C. R., J. R. Sellers, and K. C. Facemyer. 1995. Two heads are required for phosphorylation-dependent regulation of smooth muscle myosin. J. Biol. Chem. 270:2171-2175.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2171-2175
    • Cremo, C.R.1    Sellers, J.R.2    Facemyer, K.C.3
  • 10
    • 0030976860 scopus 로고    scopus 로고
    • The in vitro motility activity of beta-cardiac myosin depends on the nature of the beta-myosin heavy chain gene mutation in hypertrophic cardiomyopathy
    • Cuda, G., L. Fananapazir, N. D. Epstein, and J. R. Sellers. 1997. The in vitro motility activity of beta-cardiac myosin depends on the nature of the beta-myosin heavy chain gene mutation in hypertrophic cardiomyopathy. J. Muscle. Res. Cell Motil. 18:275-283.
    • (1997) J. Muscle. Res. Cell Motil. , vol.18 , pp. 275-283
    • Cuda, G.1    Fananapazir, L.2    Epstein, N.D.3    Sellers, J.R.4
  • 11
    • 0026067741 scopus 로고
    • Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres
    • Dantzig, J. A., M. G. Hibberd, D. R. Trentham, and Y. E. Goldman. 1991. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres. J. Physiol. 432: 639-680.
    • (1991) J. Physiol. , vol.432 , pp. 639-680
    • Dantzig, J.A.1    Hibberd, M.G.2    Trentham, D.R.3    Goldman, Y.E.4
  • 12
    • 0025014811 scopus 로고
    • Complementation of myosin null mutants in Dictyostelium discoideum by direct functional selection
    • Egelhoff, T. T, D. J. Manstein, and J. A. Spudich. 1990. Complementation of myosin null mutants in Dictyostelium discoideum by direct functional selection. Dev. Biol. 137:359-367.
    • (1990) Dev. Biol. , vol.137 , pp. 359-367
    • Egelhoff, T.T.1    Manstein, D.J.2    Spudich, J.A.3
  • 13
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg, E., and L. E. Greene. 1980. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42:209-309.
    • (1980) Annu. Rev. Physiol. , vol.42 , pp. 209-309
    • Eisenberg, E.1    Greene, L.E.2
  • 14
    • 0023251027 scopus 로고
    • Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: Effects of reversible phosphorylation on myosin structure and function
    • Griffith, L. M., S. M. Downs, and J. A. Spudich. 1987. Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function. J. Cell Biol. 104:1309-1323.
    • (1987) J. Cell Biol. , vol.104 , pp. 1309-1323
    • Griffith, L.M.1    Downs, S.M.2    Spudich, J.A.3
  • 15
    • 0010299503 scopus 로고    scopus 로고
    • Double-headed smooth and skeletal myosins generate displacements by cooperative action of the two heads
    • Guilford, W. H., D. E. Dupuis, D. M. Warshaw, G. S. Waller, K. M. Trybus, and S. Lowey. 1998. Double-headed smooth and skeletal myosins generate displacements by cooperative action of the two heads. Biophys. J. 74:A225
    • (1998) Biophys. J. , vol.74
    • Guilford, W.H.1    Dupuis, D.E.2    Warshaw, D.M.3    Waller, G.S.4    Trybus, K.M.5    Lowey, S.6
  • 16
    • 0023145911 scopus 로고
    • Sliding movement of single actin filaments on one-headed myosin filaments
    • Harada, Y., A. Noguchi, A. Kishino, and T. Yanagida. 1987. Sliding movement of single actin filaments on one-headed myosin filaments. Nature. 326:805-808.
    • (1987) Nature , vol.326 , pp. 805-808
    • Harada, Y.1    Noguchi, A.2    Kishino, A.3    Yanagida, T.4
  • 17
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada, Y., K. Sakurada, T. Aoki, D. D. Thomas, and T. Yanagida. 1990. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol Biol. 216:49-68.
    • (1990) J. Mol Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 18
    • 0030606512 scopus 로고    scopus 로고
    • Is the lever arm of myosin a molecular elastic element?
    • Howard, J, and J. A. Spudich. 1996. Is the lever arm of myosin a molecular elastic element? Proc. Natl. Acad. Sci. USA. 93:4462-4464.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4462-4464
    • Howard, J.1    Spudich, J.A.2
  • 19
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:255-318.
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 21
    • 0032079394 scopus 로고    scopus 로고
    • Quick-freeze deep-etch electron microscopy of the actin-heavy meromyosin complex during the in vitro motility assay
    • Katayama, E. 1998. Quick-freeze deep-etch electron microscopy of the actin-heavy meromyosin complex during the in vitro motility assay. J. Mol. Biol. 278:349-367.
    • (1998) J. Mol. Biol. , vol.278 , pp. 349-367
    • Katayama, E.1
  • 22
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified Malachite Green method for determination of inorganic phosphate
    • Kodama, T., K. Fukui, and K. Kometani. 1986. The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified Malachite Green method for determination of inorganic phosphate. J. Biochem. 99:1465-1472.
    • (1986) J. Biochem. , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 23
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron, S. J., and J. A. Spudich. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA. 83: 6272-6276.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 24
    • 0025782977 scopus 로고
    • Assays for actin sliding movement over myosin-coated surfaces
    • Kron, S. J., Y. Y. Toyoshima, T. Q. P. Uyeda, and J. A. Spudich. 1991. Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol. 196:399-416.
    • (1991) Methods Enzymol. , vol.196 , pp. 399-416
    • Kron, S.J.1    Toyoshima, Y.Y.2    Uyeda, T.Q.P.3    Spudich, J.A.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 26
    • 0024960744 scopus 로고
    • Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum
    • Manstein, D. J., K. M. Ruppel, and J. A. Spudich. 1989. Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum. Science. 246:656-658.
    • (1989) Science , vol.246 , pp. 656-658
    • Manstein, D.J.1    Ruppel, K.M.2    Spudich, J.A.3
  • 27
    • 0015914687 scopus 로고
    • Substructure of the myosin molecule: IV. Interaction of myosin and its subfragments with adenosine triphosphate and F-actin
    • Margossian, S. S., and S. Lowey. 1973. Substructure of the myosin molecule: IV. Interaction of myosin and its subfragments with adenosine triphosphate and F-actin. J. Mol. Biol. 74:313-330.
    • (1973) J. Mol. Biol. , vol.74 , pp. 313-330
    • Margossian, S.S.1    Lowey, S.2
  • 28
    • 0028927535 scopus 로고
    • Requirement of the two-headed structure for the phosphorylation dependent regulation of smooth muscle myosin
    • Matsu-rua, M., and M. Ikebe. 1995. Requirement of the two-headed structure for the phosphorylation dependent regulation of smooth muscle myosin. FEBS Lett. 363:246-250.
    • (1995) FEBS Lett. , vol.363 , pp. 246-250
    • Matsu-rua, M.1    Ikebe, M.2
  • 30
    • 0024554122 scopus 로고
    • Evidence for the association between two myosin heads in rigor acto-smooth muscle heavy meromyosin
    • Onishi, H., T. Maita, G. Matsuda, and K. Fujiwara. 1989. Evidence for the association between two myosin heads in rigor acto-smooth muscle heavy meromyosin. Biochemistry. 28:1898-1904.
    • (1989) Biochemistry , vol.28 , pp. 1898-1904
    • Onishi, H.1    Maita, T.2    Matsuda, G.3    Fujiwara, K.4
  • 31
    • 0025065292 scopus 로고
    • Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross- linking between the two heads of rigor smooth muscle heavy meromyosin
    • Onishi, H., T. Maita, G. Matsuda, and K. Fujiwara. 1990. Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross- linking between the two heads of rigor smooth muscle heavy meromyosin. J. Biol. Chem. 265:19362-19368.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19362-19368
    • Onishi, H.1    Maita, T.2    Matsuda, G.3    Fujiwara, K.4
  • 32
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular-weight components of myosin
    • Perrie, W. T., and S. V. Perry. 1970. An electrophoretic study of the low-molecular-weight components of myosin. Biochem. J. 119:31-38.
    • (1970) Biochem. J. , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 33
    • 0023019582 scopus 로고
    • Different phosphorylated forms of myosin in contracting tracheal smooth muscle
    • Persechini, A., K. E. Kamm, and J. T. Stull. 1986. Different phosphorylated forms of myosin in contracting tracheal smooth muscle. J. Biol. Chem. 261:6293-6299.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6293-6299
    • Persechini, A.1    Kamm, K.E.2    Stull, J.T.3
  • 35
    • 0028284391 scopus 로고
    • Role of highly conserved lysine 130 of myosin motor domain
    • Ruppel, K. M., T. Q. P. Uyeda, and J. A. Spudich. 1994. Role of highly conserved lysine 130 of myosin motor domain. J. Biol. Chem. 269: 18773-18780.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18773-18780
    • Ruppel, K.M.1    Uyeda, T.Q.P.2    Spudich, J.A.3
  • 36
    • 0345395932 scopus 로고    scopus 로고
    • Structure-function relationship of Dictyostelium myosin motor
    • Shimada, T., and K. Sutoh. 1996. Structure-function relationship of Dictyostelium myosin motor. Cell Struct. Func. 21:598.
    • (1996) Cell Struct. Func. , vol.21 , pp. 598
    • Shimada, T.1    Sutoh, K.2
  • 37
    • 0029962710 scopus 로고    scopus 로고
    • Activation of Dictyostelium myosin light chain kinase A by phosphorylation of Thr 166
    • Smith, J. L., L. A. Silveira, and J. A. Spudich. 1996. Activation of Dictyostelium myosin light chain kinase A by phosphorylation of Thr 166. EMBO J. 22:6075-83.
    • (1996) EMBO J. , vol.22 , pp. 6075-6083
    • Smith, J.L.1    Silveira, L.A.2    Spudich, J.A.3
  • 38
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction: I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction: I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 42
    • 0027767689 scopus 로고
    • A functional recombinant myosin II lacking a regulatory light chain-binding site
    • Uyeda, T. Q. P., and J. A. Spudich. 1993. A functional recombinant myosin II lacking a regulatory light chain-binding site. Science. 262:1867-1870.
    • (1993) Science , vol.262 , pp. 1867-1870
    • Uyeda, T.Q.P.1    Spudich, J.A.2
  • 43
    • 0025900542 scopus 로고
    • Quantized velocities at low myosin densities in an in vitro motility assay
    • Uyeda, T. Q. P., H. M. Warrick, S. J. Kron, and J. A. Spudich. 1991. Quantized velocities at low myosin densities in an in vitro motility assay. Nature. 352:307-311.
    • (1991) Nature , vol.352 , pp. 307-311
    • Uyeda, T.Q.P.1    Warrick, H.M.2    Kron, S.J.3    Spudich, J.A.4
  • 44
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale, R. D., T. Funatsu, D. W. Pierce, L. Romberg, Y. Harada, and T. Yanagida. 1996. Direct observation of single kinesin molecules moving along microtubules. Nature. 380:451-453.
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 45
    • 0023484279 scopus 로고
    • Myosin structure and function in cell motility
    • Warrick, H. M., and J. A. Spudich. 1987. Myosin structure and function in cell motility. Annu. Rev. Cell Biol. 3:379-421.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 379-421
    • Warrick, H.M.1    Spudich, J.A.2
  • 46
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw, D. M., J. M. Derosiers, S. S. Work, and K. M. Trybus. 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    Derosiers, J.M.2    Work, S.S.3    Trybus, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.