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Volumn 346, Issue 2, 2005, Pages 189-200

Quantitative atomic force microscopy image analysis of unusual filaments formed by the Acanthamoeba castellanii myosin II rod domain

Author keywords

Atomic force microscopy; Coiled coil; Myosin; Rod domain

Indexed keywords

ANTIBODIES; ATOMIC FORCE MICROSCOPY;

EID: 27644482403     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.08.026     Document Type: Article
Times cited : (10)

References (31)
  • 1
    • 0020355696 scopus 로고
    • Structure and polymerization of Acanthamoeba myosin-II filaments
    • T.D. Pollard Structure and polymerization of Acanthamoeba myosin-II filaments J. Cell Biol. 95 1982 816 825
    • (1982) J. Cell Biol. , vol.95 , pp. 816-825
    • Pollard, T.D.1
  • 3
    • 0022638045 scopus 로고
    • Macromolecular assemblies of myosin
    • E. Reisler, P. Cheung, and N. Borochov Macromolecular assemblies of myosin Biophys. J. 49 1986 335 342
    • (1986) Biophys. J. , vol.49 , pp. 335-342
    • Reisler, E.1    Cheung, P.2    Borochov, N.3
  • 4
    • 0021250602 scopus 로고
    • Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength
    • K.M. Trybus, and S. Lowey Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength J. Biol. Chem. 259 1984 8564 8571
    • (1984) J. Biol. Chem. , vol.259 , pp. 8564-8571
    • Trybus, K.M.1    Lowey, S.2
  • 6
    • 0024747004 scopus 로고
    • The mechanism of assembly of Acanthamoeba myosin-II minifilaments: Minifilaments assemble by three successive dimerization steps
    • J.H. Sinard, W.F. Stafford, and T.D. Pollard The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps J. Cell Biol. 109 1989 1537 1547
    • (1989) J. Cell Biol. , vol.109 , pp. 1537-1547
    • Sinard, J.H.1    Stafford, W.F.2    Pollard, T.D.3
  • 7
    • 0021920589 scopus 로고
    • Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II
    • J. Kuznicki, G.P. Cote, B. Bowers, and E.D. Korn Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II J. Biol. Chem. 260 1985 1967 1972
    • (1985) J. Biol. Chem. , vol.260 , pp. 1967-1972
    • Kuznicki, J.1    Cote, G.P.2    Bowers, B.3    Korn, E.D.4
  • 8
    • 0024291215 scopus 로고
    • Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail
    • M.A.L. Atkinson, E. Appella, M.A. Corigliano-Murphy, and E.D. Korn Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail FEBS Lett. 234 1988 435 438
    • (1988) FEBS Lett. , vol.234 , pp. 435-438
    • Atkinson, M.A.L.1    Appella, E.2    Corigliano-Murphy, M.A.3    Korn, E.D.4
  • 9
    • 0025666497 scopus 로고
    • Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins, I. High resolution epitope mapping and characterization of monoclonal antibody binding sites
    • D.L. Rimm, D.A. Kaiser, D. Bhandari, P. Maupin, D.P. Kiehart, and T.D. Pollard Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins, I. High resolution epitope mapping and characterization of monoclonal antibody binding sites J. Cell Biol. 111 1990 2405 2416
    • (1990) J. Cell Biol. , vol.111 , pp. 2405-2416
    • Rimm, D.L.1    Kaiser, D.A.2    Bhandari, D.3    Maupin, P.4    Kiehart, D.P.5    Pollard, T.D.6
  • 11
    • 0023587876 scopus 로고
    • Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: Evidence of a hinge in the rodlike tail
    • J.A. Hammer, B. Bowers, B.M. Paterson, and E.D. Korn Complete nucleotide sequence and deduced polypeptide sequence of a nonmuscle myosin heavy chain gene from Acanthamoeba: evidence of a hinge in the rodlike tail J. Cell Biol. 105 1987 913 925
    • (1987) J. Cell Biol. , vol.105 , pp. 913-925
    • Hammer, J.A.1    Bowers, B.2    Paterson, B.M.3    Korn, E.D.4
  • 12
    • 0030872273 scopus 로고    scopus 로고
    • Two-state thermal unfolding of a long dimeric coiled-coil: The Acanthamoeba myosin II rod
    • M. Zolkiewski, M.J. Redowicz, E. Korn, J. Hammer, and A. Ginsburg Two-state thermal unfolding of a long dimeric coiled-coil: the Acanthamoeba myosin II rod Biochemistry 36 1997 7876 7883
    • (1997) Biochemistry , vol.36 , pp. 7876-7883
    • Zolkiewski, M.1    Redowicz, M.J.2    Korn, E.3    Hammer, J.4    Ginsburg, A.5
  • 13
    • 1042291877 scopus 로고    scopus 로고
    • MgATP-induced conformational changes in a single myosin molecule observed by atomic force microscopy: Periodicity of substructures in myosin rods
    • M. Taniguchi, O. Matsumoto, S. Suzuki, Y. Nishino, A. Okuda, T. Taga, and T. Yamane MgATP-induced conformational changes in a single myosin molecule observed by atomic force microscopy: periodicity of substructures in myosin rods Scanning 25 2003 223 229
    • (2003) Scanning , vol.25 , pp. 223-229
    • Taniguchi, M.1    Matsumoto, O.2    Suzuki, S.3    Nishino, Y.4    Okuda, A.5    Taga, T.6    Yamane, T.7
  • 14
    • 0031056521 scopus 로고    scopus 로고
    • Cryo-atomic force microscopy of smooth muscle myosin
    • Y. Zhang, Z. Shao, A.P. Somlyo, and A.V. Somlyo Cryo-atomic force microscopy of smooth muscle myosin Biophys. J. 72 1997 1308 1318
    • (1997) Biophys. J. , vol.72 , pp. 1308-1318
    • Zhang, Y.1    Shao, Z.2    Somlyo, A.P.3    Somlyo, A.V.4
  • 15
    • 0028905551 scopus 로고
    • Atomic force microscopy of the myosin molecule
    • P. Hallett, G. Offer, and M.J. Miles Atomic force microscopy of the myosin molecule Biophys. J. 68 1995 1604 1606
    • (1995) Biophys. J. , vol.68 , pp. 1604-1606
    • Hallett, P.1    Offer, G.2    Miles, M.J.3
  • 16
    • 0022419381 scopus 로고
    • Negative staining of myosin molecules
    • M. Walker, P. Knight, and J. Trinick Negative staining of myosin molecules J. Mol. Biol. 184 1985 535 542
    • (1985) J. Mol. Biol. , vol.184 , pp. 535-542
    • Walker, M.1    Knight, P.2    Trinick, J.3
  • 18
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • M.L. Johnson, J.J. Correia, D.A. Yphantis, and H.R. Halvorson Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques Biophys. J. 36 1981 575 588
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 19
    • 0003425844 scopus 로고
    • Chapter 4, Chapman & Hall, London
    • U.W. Gedde, Polymer Physics, Chapter 4, Chapman & Hall, London, 1995.
    • (1995) Polymer Physics
    • Gedde, U.W.1
  • 20
    • 0035800344 scopus 로고    scopus 로고
    • On the distribution of fragment sizes in the fragmentation of polymer chains
    • B.C. Hathorn, B.G. Sumpter, and D.W. Noid On the distribution of fragment sizes in the fragmentation of polymer chains Macromol. Theory Simul. 10 2001 587 591
    • (2001) Macromol. Theory Simul. , vol.10 , pp. 587-591
    • Hathorn, B.C.1    Sumpter, B.G.2    Noid, D.W.3
  • 21
    • 0035501163 scopus 로고    scopus 로고
    • Enhanced Imaging of DNA via active quality factor control
    • A.D.L. Humphris, A.N. Round, and M.J. Miles Enhanced Imaging of DNA via active quality factor control Surface Sci. 491 2001 468 472
    • (2001) Surface Sci. , vol.491 , pp. 468-472
    • Humphris, A.D.L.1    Round, A.N.2    Miles, M.J.3
  • 22
    • 0027657356 scopus 로고
    • Envelope reconstruction of probe microscope images
    • D.J. Keller, and F.S. Franke Envelope reconstruction of probe microscope images Surface Sci. 294 1993 409 419
    • (1993) Surface Sci. , vol.294 , pp. 409-419
    • Keller, D.J.1    Franke, F.S.2
  • 24
    • 0027199086 scopus 로고
    • Colloidal gold particles as an incompressible atomic force microscopy imaging standard for assessing the compressibility of biomolecule
    • J. Vesenka, S. Manne, R. Giverson, T. Marsh, and E. Henderson Colloidal gold particles as an incompressible atomic force microscopy imaging standard for assessing the compressibility of biomolecule Biophys. J. 65 1993 992 997
    • (1993) Biophys. J. , vol.65 , pp. 992-997
    • Vesenka, J.1    Manne, S.2    Giverson, R.3    Marsh, T.4    Henderson, E.5
  • 25
    • 0020486796 scopus 로고
    • The myosin dimer: An intermediate in the self-assembly of the thick filament of vertebrate skeletal muscle
    • J.S. Davis, J. Buck, and E.P. Greene The myosin dimer: an intermediate in the self-assembly of the thick filament of vertebrate skeletal muscle FEBS Lett. 140 1982 293 297
    • (1982) FEBS Lett. , vol.140 , pp. 293-297
    • Davis, J.S.1    Buck, J.2    Greene, E.P.3
  • 26
    • 0014498776 scopus 로고
    • Physicochemical studies on the aggregation of bovine cardiac tropomyosin with ionic strength
    • W.D. McCubbin, and C.M. Kay Physicochemical studies on the aggregation of bovine cardiac tropomyosin with ionic strength Can. J. Biochem. 47 1969 411 414
    • (1969) Can. J. Biochem. , vol.47 , pp. 411-414
    • McCubbin, W.D.1    Kay, C.M.2
  • 27
    • 0037127219 scopus 로고    scopus 로고
    • Quantitative analysis of tropomyosin linear polymerization equilibrium as a function of ionic strength
    • A.D. Sousa, and C.S. Farah Quantitative analysis of tropomyosin linear polymerization equilibrium as a function of ionic strength J. Biol. Chem. 277 2002 2081 2088
    • (2002) J. Biol. Chem. , vol.277 , pp. 2081-2088
    • Sousa, A.D.1    Farah, C.S.2
  • 28
    • 0017136639 scopus 로고
    • The 14-fold periodicity in alpha-tropomyosin and the interaction with actin
    • A.D. McLachlan, and M. Stewart The 14-fold periodicity in alpha-tropomyosin and the interaction with actin J. Mol. Biol. 103 1976 271 298
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 29
    • 0019873745 scopus 로고
    • Structure of rabbit skeletal myosin. Analysis of the amino acid sequences of two fragments from the rod region
    • D.A.D. Parry Structure of rabbit skeletal myosin. Analysis of the amino acid sequences of two fragments from the rod region J. Mol. Biol. 153 1981 459 464
    • (1981) J. Mol. Biol. , vol.153 , pp. 459-464
    • Parry, D.A.D.1
  • 30
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • A.D. McLachlan, and J. Karn Periodic features in the amino acid sequence of nematode myosin rod J. Mol. Biol. 164 1983 605 626
    • (1983) J. Mol. Biol. , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 31
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • A.D. McLachlan, and M. Stewart Tropomyosin coiled-coil interactions: evidence for an unstaggered structure J. Mol. Biol. 98 1975 293 304
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2


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