메뉴 건너뛰기




Volumn 23, Issue 7-8, 2002, Pages 685-795

Amino acids 519-524 of Dictyostelium myosin II form a surface loop that aids actin binding by facilitating a conformational change

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; MUTANT PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II;

EID: 0042020001     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1024463325335     Document Type: Article
Times cited : (4)

References (38)
  • 2
    • 0033545955 scopus 로고    scopus 로고
    • Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region
    • Batra R, Geeves MA and Manstein DJ (1999) Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region. Biochemistry 38: 6126-6134.
    • (1999) Biochemistry , vol.38 , pp. 6126-6134
    • Batra, R.1    Geeves, M.A.2    Manstein, D.J.3
  • 3
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres
    • Dantzig JA, Goldman YE, Millar NC, Lacktis J and Homsher E (1992) Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol 451: 247-278.
    • (1992) J Physiol , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Lacktis, J.4    Homsher, E.5
  • 4
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
    • De Lozanne A and Spudich JA (1987) Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236: 1086-1091.
    • (1987) Science , vol.236 , pp. 1086-1091
    • De Lozanne, A.1    Spudich, J.A.2
  • 5
    • 0027372314 scopus 로고
    • Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo
    • Egelhoff TT, Lee RJ and Spudich JA (1993) Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo. Cell 75: 363-371.
    • (1993) Cell , vol.75 , pp. 363-371
    • Egelhoff, T.T.1    Lee, R.J.2    Spudich, J.A.3
  • 7
    • 0029159959 scopus 로고
    • X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4
    • Fisher AJ, Smith CA, Thoden JB, Smith R, Sutoh K, Holden HM and Rayment I (1995) X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4. Biochemistry 34: 8960-8972.
    • (1995) Biochemistry , vol.34 , pp. 8960-8972
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.B.3    Smith, R.4    Sutoh, K.5    Holden, H.M.6    Rayment, I.7
  • 8
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch M, Geeves MA and Manstein DJ (1998) Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry 37: 6317-6326.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 9
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves MA and Holmes KC (1999) Structural mechanism of muscle contraction. Annu Rev Biochem 68: 687-728.
    • (1999) Annu Rev Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 10
    • 0017137847 scopus 로고
    • Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin
    • Gordon DJ, Yang YZ and Korn ED (1976) Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin. J Biol Chem 251: 7474-7479.
    • (1976) J Biol Chem , vol.251 , pp. 7474-7479
    • Gordon, D.J.1    Yang, Y.Z.2    Korn, E.D.3
  • 11
    • 0022463569 scopus 로고
    • Relationships between chemical and mechanical events during muscular contraction
    • Hibberd MG and Trentham DR (1986) Relationships between chemical and mechanical events during muscular contraction. Ann Rev Biophys Biophys Chem 15: 119-161.
    • (1986) Ann Rev Biophys Biophys Chem , vol.15 , pp. 119-161
    • Hibberd, M.G.1    Trentham, D.R.2
  • 12
    • 0023189474 scopus 로고
    • Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum
    • Knecht DA and Loomis WF (1987) Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science 236: 1081-1086.
    • (1987) Science , vol.236 , pp. 1081-1086
    • Knecht, D.A.1    Loomis, W.F.2
  • 13
    • 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, Fukui K and Kometani K (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
  • 14
    • 0035936553 scopus 로고    scopus 로고
    • Functional roles of ionic and hydrophobic surface loops in smooth muscle myosin: Their interactions with actin
    • Kojima S, Konishi K, Katoh K, Fujiwara K, Martinez HM, Morales MF and Onishi H (2001) Functional roles of ionic and hydrophobic surface loops in smooth muscle myosin: their interactions with actin. Biochemistry 40: 657-664.
    • (2001) Biochemistry , vol.40 , pp. 657-664
    • Kojima, S.1    Konishi, K.2    Katoh, K.3    Fujiwara, K.4    Martinez, H.M.5    Morales, M.F.6    Onishi, H.7
  • 15
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T and Mihashi K (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114: 33-38.
    • (1981) Eur J Biochem , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 16
    • 0034728772 scopus 로고    scopus 로고
    • Involvement of tail domains in regulation of Dictyostelium myosin II
    • Liu X, Ito K, Lee RJ and Uyeda TQP (2000) Involvement of tail domains in regulation of Dictyostelium myosin II. Biochem Biophys Res Comm 271: 75-81.
    • (2000) Biochem Biophys Res Comm , vol.271 , pp. 75-81
    • Liu, X.1    Ito, K.2    Lee, R.J.3    Uyeda, T.Q.P.4
  • 17
    • 0032564352 scopus 로고    scopus 로고
    • Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation
    • Liu X, Ito K, Morimoto S, Hikkoshi-Iwane A, Yanagida T and Uyeda TQP (1998) Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation. Proc Natl Acad Sci USA 95: 14,124-14,129.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14124-14129
    • Liu, X.1    Ito, K.2    Morimoto, S.3    Hikkoshi-Iwane, A.4    Yanagida, T.5    Uyeda, T.Q.P.6
  • 18
    • 0032087613 scopus 로고    scopus 로고
    • Conditional loss-of-myosin-II-function mutants reveal a position in the tail that is critical for filament nucleation
    • Moores SL and Spudich JA (1998) Conditional loss-of-myosin-II-function mutants reveal a position in the tail that is critical for filament nucleation. Mol Cell 1: 1043-1050.
    • (1998) Mol Cell , vol.1 , pp. 1043-1050
    • Moores, S.L.1    Spudich, J.A.2
  • 19
    • 0031879662 scopus 로고    scopus 로고
    • Intragenic suppressors of Dictyostelium myosin G680 mutants demarcate discrete structural elements. Implications for conformational states of the motor
    • Patterson B (1998) Intragenic suppressors of Dictyostelium myosin G680 mutants demarcate discrete structural elements. Implications for conformational states of the motor. Genetics 149: 1799-1807.
    • (1998) Genetics , vol.149 , pp. 1799-1807
    • Patterson, B.1
  • 20
    • 0034429853 scopus 로고    scopus 로고
    • Genetic techniques for enhancing biochemical and structural characterization of Dictyostelium myosin II
    • Patterson B (2000) Genetic techniques for enhancing biochemical and structural characterization of Dictyostelium myosin II. Methods 22: 299-306.
    • (2000) Methods , vol.22 , pp. 299-306
    • Patterson, B.1
  • 21
    • 0026235027 scopus 로고
    • Molecular genetic approaches to the cytoskeleton in Dictyostelium
    • Patterson B, Ruppel KM and Spudich JA (1991) Molecular genetic approaches to the cytoskeleton in Dictyostelium. Curr Opin Genet Dev 1: 378-382.
    • (1991) Curr Opin Genet Dev , vol.1 , pp. 378-382
    • Patterson, B.1    Ruppel, K.M.2    Spudich, J.A.3
  • 22
    • 0030836303 scopus 로고    scopus 로고
    • Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects
    • Patterson B, Ruppel KM, Wu Y and Spudich JA (1997) Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects. J Biol Chem 272: 27,612-27,617.
    • (1997) J Biol Chem , vol.272 , pp. 27612-27617
    • Patterson, B.1    Ruppel, K.M.2    Wu, Y.3    Spudich, J.A.4
  • 24
    • 0027267667 scopus 로고
    • Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum
    • Ritchie MD, Geeves MA, Woodward SK and Manstein DJ (1993) Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum. Proc Natl Acad Sci USA 90: 8619-8623.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8619-8623
    • Ritchie, M.D.1    Geeves, M.A.2    Woodward, S.K.3    Manstein, D.J.4
  • 25
    • 0030035665 scopus 로고    scopus 로고
    • Structure-function studies of the myosin motor domain: Importance of the 50-kDa cleft
    • Ruppel KM and Spudich JA (1996) Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft. Mol Biol Cell 7: 1123-1136.
    • (1996) Mol Biol Cell , vol.7 , pp. 1123-1136
    • Ruppel, K.M.1    Spudich, J.A.2
  • 26
    • 0028284391 scopus 로고
    • Role of highly conserved lysine 130 of myosin motor domain
    • Ruppel KM, Uyeda TQP and Spudich JA (1994) Role of highly conserved lysine 130 of myosin motor domain. J Biol Chem 269: 18,773-18,780.
    • (1994) J Biol Chem , vol.269 , pp. 18773-18780
    • Ruppel, K.M.1    Uyeda, T.Q.P.2    Spudich, J.A.3
  • 27
    • 0033621469 scopus 로고    scopus 로고
    • Deletion of the myopathy loop of Dictyostelium myosin II and its impact on motor functions
    • Sasaki N, Asukagawa H, Yasuda R, Hiratsuka T and Sutoh K (1999) Deletion of the myopathy loop of Dictyostelium myosin II and its impact on motor functions. J Biol Chem 274: 37,840-37,844.
    • (1999) J Biol Chem , vol.274 , pp. 37840-37844
    • Sasaki, N.1    Asukagawa, H.2    Yasuda, R.3    Hiratsuka, T.4    Sutoh, K.5
  • 29
    • 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 CA and 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: 5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 30
    • 0029962710 scopus 로고    scopus 로고
    • Activation of Dictyostelium myosin light chain kinase A by phosphorylation of Thr166
    • Smith JL, Silveira LA and Spudich JA (1996) Activation of Dictyostelium myosin light chain kinase A by phosphorylation of Thr166. EMBO J 15: 6075-6083.
    • (1996) EMBO J , vol.15 , pp. 6075-6083
    • Smith, J.L.1    Silveira, L.A.2    Spudich, J.A.3
  • 31
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA and Watt S (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin 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
  • 32
    • 0023073916 scopus 로고
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions
    • Spudich JA (ed). Academic Press, Orlando
    • Sussman M (1987) Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions. In: Spudich JA (ed) Dictyostelium discoideum: Molecular Approaches to Cell Biology. (vol. 28, pp. 9-29) Academic Press, Orlando.
    • (1987) Dictyostelium discoideum: Molecular Approaches to Cell Biology , vol.28 , pp. 9-29
    • Sussman, M.1
  • 33
    • 0020563473 scopus 로고
    • Mapping of actin-binding sites on the heavy chain of myosin subfragment-1
    • Sutoh K (1983) Mapping of actin-binding sites on the heavy chain of myosin subfragment-1. Biochemistry 22: 1579-1585.
    • (1983) Biochemistry , vol.22 , pp. 1579-1585
    • Sutoh, K.1
  • 34
    • 0024991350 scopus 로고
    • Myosin step size: Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • Uyeda TQP, Kron SJ and Spudich JA (1990) Myosin step size: estimation from slow sliding movement of actin over low densities of heavy meromyosin. J Mol Biol 214: 699-710.
    • (1990) J Mol Biol , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 35
    • 0037199470 scopus 로고    scopus 로고
    • Evidence for a novel, strongly bound aeto-S1 complex carrying ADP and phosphate stabilized in the G680V mutant of Dictyostelium myosin II
    • Uyeda TQP, Tokuraku K, Kaseda K, Webb MR and Patterson B (2002) Evidence for a novel, strongly bound aeto-S1 complex carrying ADP and phosphate stabilized in the G680V mutant of Dictyostelium myosin II. Biochemistry 41: 9525-9534.
    • (2002) Biochemistry , vol.41 , pp. 9525-9534
    • Uyeda, T.Q.P.1    Tokuraku, K.2    Kaseda, K.3    Webb, M.R.4    Patterson, B.5
  • 36
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw HM, Derosiers JM, Work SS and Trybus KM (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, H.M.1    Derosiers, J.M.2    Work, S.S.3    Trybus, K.M.4
  • 37
    • 0032867566 scopus 로고    scopus 로고
    • Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release
    • Wu Y, Nejad M and Patterson B (1999) Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release. Genetics 153: 107-116.
    • (1999) Genetics , vol.153 , pp. 107-116
    • Wu, Y.1    Nejad, M.2    Patterson, B.3
  • 38
    • 0030868951 scopus 로고    scopus 로고
    • Transport of myosin II to the equatorial region without its own motor activity in mitotic Dictyostelium cells
    • Yumura S and Uyeda TQP (1997) Transport of myosin II to the equatorial region without its own motor activity in mitotic Dictyostelium cells. Mol Biol Cell 8: 2089-2099.
    • (1997) Mol Biol Cell , vol.8 , pp. 2089-2099
    • Yumura, S.1    Uyeda, T.Q.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.