메뉴 건너뛰기




Volumn 123, Issue 1, 1998, Pages 8-16

Electron microscopic observation of monomeric actin attached to a myosin head

Author keywords

Actin myosin interface; Actomyosin complex; Chemical crosslinking; G actin; Low angle rotary shadowing

Indexed keywords

ACTIN; MYOSIN;

EID: 0032170751     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.4019     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 0027718079 scopus 로고
    • Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin
    • Andreeva, A. L., Andreev, O. A., and Borejdo, J. (1993) Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin, Biochemistry 32, 13956-13960.
    • (1993) Biochemistry , vol.32 , pp. 13956-13960
    • Andreeva, A.L.1    Andreev, O.A.2    Borejdo, J.3
  • 2
    • 0023042686 scopus 로고
    • Structure of the actin-myosin complex produced by crosslinking in the presence of ATP
    • Arata, T. (1986) Structure of the actin-myosin complex produced by crosslinking in the presence of ATP, J. Mol. Biol. 191, 107-116.
    • (1986) J. Mol. Biol. , vol.191 , pp. 107-116
    • Arata, T.1
  • 3
    • 0025966670 scopus 로고
    • Interaction of nonpolymerizable actins with myosin
    • Arata, T. (1991) Interaction of nonpolymerizable actins with myosin, J. Biochem. 109, 335-340.
    • (1991) J. Biochem. , vol.109 , pp. 335-340
    • Arata, T.1
  • 4
    • 0030466870 scopus 로고    scopus 로고
    • A myosin head can interact with two chemically modified G-actin monomers at ATP-modulated multiple sites
    • Arata, T. (1996) A myosin head can interact with two chemically modified G-actin monomers at ATP-modulated multiple sites, Biochemistry 35, 16061-16068.
    • (1996) Biochemistry , vol.35 , pp. 16061-16068
    • Arata, T.1
  • 5
    • 0028306266 scopus 로고
    • The covalent maleimidobenzoyl-actin-myosin head complex: Cross-linking of the 50 kDa heavy chain region to actin subdomain-2
    • Bertrand, R., Derancourt, J., and Kassab, R. (1994) The covalent maleimidobenzoyl-actin-myosin head complex: Cross-linking of the 50 kDa heavy chain region to actin subdomain-2, FEBS Lett. 345, 113-119.
    • (1994) FEBS Lett. , vol.345 , pp. 113-119
    • Bertrand, R.1    Derancourt, J.2    Kassab, R.3
  • 6
    • 0030820679 scopus 로고    scopus 로고
    • Probing the hydrodynamic interactions in the skeletal actomyosin subfragment 1 and its nucleotide complexes by zero-length cross-linking with a nickel-peptide chelate
    • Bertrand, R., Derancourt, J., and Kassab, R. (1997) Probing the hydrodynamic interactions in the skeletal actomyosin subfragment 1 and its nucleotide complexes by zero-length cross-linking with a nickel-peptide chelate, Biochemistry 36, 9703-9714.
    • (1997) Biochemistry , vol.36 , pp. 9703-9714
    • Bertrand, R.1    Derancourt, J.2    Kassab, R.3
  • 7
    • 0024406414 scopus 로고
    • Coupling of nonpolymerizable monomeric actin to the F-actin-binding region of the myosin head
    • Bettache, N., Bertrand, R., and Kassab, R. (1989) Coupling of nonpolymerizable monomeric actin to the F-actin-binding region of the myosin head, Proc. Natl. Acad. Sci. USA 86, 6028-6032.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6028-6032
    • Bettache, N.1    Bertrand, R.2    Kassab, R.3
  • 8
    • 0025102695 scopus 로고
    • Maleimidobenzoyl-G-actin: Structural properties and interaction with skeletal myosin subfragment-1
    • Bettache, N., Bertrand, R., and Kassab, R. (1990) Maleimidobenzoyl-G-actin: Structural properties and interaction with skeletal myosin subfragment-1, Biochemistry 29, 9085-9091.
    • (1990) Biochemistry , vol.29 , pp. 9085-9091
    • Bettache, N.1    Bertrand, R.2    Kassab, R.3
  • 9
    • 0026515487 scopus 로고
    • Specific crosslinking of the SH1 thiol of skeletal myosin subfragment 1 to F-actin and G-actin
    • Bettache, N., Bertrand, R., and Kassab, R. (1992) Specific crosslinking of the SH1 thiol of skeletal myosin subfragment 1 to F-actin and G-actin, Biochemistry 31, 389-395.
    • (1992) Biochemistry , vol.31 , pp. 389-395
    • Bettache, N.1    Bertrand, R.2    Kassab, R.3
  • 10
    • 0028921163 scopus 로고
    • A single myosin head can be cross-linked to the N-terminal of two adjacent actin monomers
    • Bonafe, N., and Chaussepied, P. (1995) A single myosin head can be cross-linked to the N-terminal of two adjacent actin monomers, Biophys. J. 68, 35s-43s.
    • (1995) Biophys. J. , vol.68
    • Bonafe, N.1    Chaussepied, P.2
  • 11
    • 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
  • 12
    • 0024843553 scopus 로고
    • Isolation and characterization of the G-actin-myosin head complex
    • Chaussepied, P., and Kasprzak, A. A. (1989) Isolation and characterization of the G-actin-myosin head complex, Nature 342, 950-953.
    • (1989) Nature , vol.342 , pp. 950-953
    • Chaussepied, P.1    Kasprzak, A.A.2
  • 13
    • 0028919458 scopus 로고
    • Actin and the actomyosin interface: A review
    • Dos Remedios, C. G., and Moens, P. D. J. (1995) Actin and the actomyosin interface: A review, Biochim. Biophys. Acta 1228, 99-124.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 99-124
    • Dos Remedios, C.G.1    Moens, P.D.J.2
  • 14
    • 0029671280 scopus 로고    scopus 로고
    • Cross-link between cys 374 and cys 10 of actin abolishes polymerizability and allows study of the properties of the F-actin monomer
    • Heintz, D., and Faulstich, H. (1996) Cross-link between cys 374 and cys 10 of actin abolishes polymerizability and allows study of the properties of the F-actin monomer, Biochemistry 35, 258-265.
    • (1996) Biochemistry , vol.35 , pp. 258-265
    • Heintz, D.1    Faulstich, H.2
  • 15
    • 0026785574 scopus 로고
    • Binding between maleimidobenzoyl-G-actin and myosin subfragment 1
    • Hozumi, T. (1992) Binding between maleimidobenzoyl-G-actin and myosin subfragment 1, Biochemistry 31, 10070-10073.
    • (1992) Biochemistry , vol.31 , pp. 10070-10073
    • Hozumi, T.1
  • 16
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction
    • Huxley, A. F., and Niedergerke, R. (1954) Structural changes in muscle during contraction, Nature 173, 971-973.
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 17
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction
    • Huxley, H. E., and Hanson, J. (1954) Changes in the cross-striations of muscle during contraction, Nature 173, 973-976.
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.E.1    Hanson, J.2
  • 19
    • 0025260746 scopus 로고
    • Peptide mimetics of an actin-binding site on myosin span two functional domains on actin
    • Keane, A. M., Trayer, I. P., Levine, B. A., Zeugner, C., and Ruegg, J. C. (1990) Peptide mimetics of an actin-binding site on myosin span two functional domains on actin, Nature 344, 265-268.
    • (1990) Nature , vol.344 , pp. 265-268
    • Keane, A.M.1    Trayer, I.P.2    Levine, B.A.3    Zeugner, C.4    Ruegg, J.C.5
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0030832286 scopus 로고    scopus 로고
    • The structure of the acto-myosin subfragment 1 complex: Results of searches using data from electron microscopy and X-ray crystallography
    • Mendelson, R. A., and Morris, E. P. (1997) The structure of the acto-myosin subfragment 1 complex: Results of searches using data from electron microscopy and X-ray crystallography, Proc. Natl. Acad. Sci. USA 94, 8533-8538.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8533-8538
    • Mendelson, R.A.1    Morris, E.P.2
  • 23
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan, R. A. (1996) Protein-protein interactions in the rigor actomyosin complex, Proc. Natl. Acad. Sci. USA 93, 21-26.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 24
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, tropomyosin revealed by cryo-electron microscopy
    • Milligan, R., and Flicker, P. F. (1987) Structural relationships of actin, myosin, tropomyosin revealed by cryo-electron microscopy, J. Cell Biol. 105, 29-39.
    • (1987) J. Cell Biol. , vol.105 , pp. 29-39
    • Milligan, R.1    Flicker, P.F.2
  • 25
    • 85030340815 scopus 로고
    • Cardiac myosin can make actin filament bundles
    • Miyanishi, T., Hayashibara, T., and Maita, T. (1995) Cardiac myosin can make actin filament bundles, Biophys. J. 68, A162.
    • (1995) Biophys. J. , vol.68
    • Miyanishi, T.1    Hayashibara, T.2    Maita, T.3
  • 26
    • 0019447576 scopus 로고
    • Structure of the actin-myosin interface
    • Mornet, D., Bertrand, R., Audemard, E., and Kassab, R. (1981) Structure of the actin-myosin interface, Nature 292, 301-306.
    • (1981) Nature , vol.292 , pp. 301-306
    • Mornet, D.1    Bertrand, R.2    Audemard, E.3    Kassab, R.4
  • 27
    • 0001697806 scopus 로고
    • Myosin adenosinetriphosphatase
    • Perry, S. V. (1955) Myosin adenosinetriphosphatase, Methods Enzymol. 2, 583-588.
    • (1955) Methods Enzymol. , vol.2 , pp. 583-588
    • Perry, S.V.1
  • 31
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction: Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and Watt, S. (1972) The regulation of rabbit skeletal muscle contraction: Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem. 246, 4866-4871.
    • (1972) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 32
    • 0020563473 scopus 로고
    • Mapping of actin-binding sites on the heavy chain of myosin
    • Sutoh, K. (1983) Mapping of actin-binding sites on the heavy chain of myosin, Biochemistry 22, 1579-1585.
    • (1983) Biochemistry , vol.22 , pp. 1579-1585
    • Sutoh, K.1
  • 33
    • 0021590825 scopus 로고
    • Electron microscopic visualization of the SH1 thiol of myosin by the use of an avidin-biotin system
    • Sutoh, K., Yamamoto, K., and Wakabayashi, T. (1984) Electron microscopic visualization of the SH1 thiol of myosin by the use of an avidin-biotin system, J. Mol. Biol. 178, 323-339.
    • (1984) J. Mol. Biol. , vol.178 , pp. 323-339
    • Sutoh, K.1    Yamamoto, K.2    Wakabayashi, T.3
  • 34
    • 0024554026 scopus 로고
    • Electron microscopic mapping of myosin head with site-directed antibodies
    • Sutoh, K., Tokunaga, M., and Wakabayashi, T. (1989) Electron microscopic mapping of myosin head with site-directed antibodies, J. Mol. Biol. 206, 357-363.
    • (1989) J. Mol. Biol. , vol.206 , pp. 357-363
    • Sutoh, K.1    Tokunaga, M.2    Wakabayashi, T.3
  • 35
    • 0028437159 scopus 로고
    • Angular disorder of weak-binding actomyosin cross-bridges
    • Thomas, D. D. (1994) Angular disorder of weak-binding actomyosin cross-bridges, Biophys. J. 66, 1272-1273.
    • (1994) Biophys. J. , vol.66 , pp. 1272-1273
    • Thomas, D.D.1
  • 36
    • 0023261634 scopus 로고
    • Location of the ATPase site of myosin determined by three-dimensional electron microscopy
    • Tokunaga, M., Sutoh, K., Toyoshima, T., and Wakabayashi, T. (1987) Location of the ATPase site of myosin determined by three-dimensional electron microscopy, Nature 329, 635-638.
    • (1987) Nature , vol.329 , pp. 635-638
    • Tokunaga, M.1    Sutoh, K.2    Toyoshima, T.3    Wakabayashi, T.4
  • 37
    • 0021914089 scopus 로고
    • Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle, V
    • Toyoshima, C., and Wakabayashi, T. (1985) Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle, V, J. Biochem. 97, 245-263.
    • (1985) J. Biochem. , vol.97 , pp. 245-263
    • Toyoshima, C.1    Wakabayashi, T.2
  • 38
    • 0026001743 scopus 로고
    • Myosin subfragment-1 interacts with two G-actin molecules in the absence of ATP
    • Valentin-Ranc, C., Combeau, C., Pantaloni, D., and Carlier, M.-F. (1991) Myosin subfragment-1 interacts with two G-actin molecules in the absence of ATP, J. Biol. Chem. 266, 17872-17879.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17872-17879
    • Valentin-Ranc, C.1    Combeau, C.2    Pantaloni, D.3    Carlier, M.-F.4
  • 39
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G., and Taylor, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin, Nature 257, 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 40
    • 0020620657 scopus 로고
    • Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis
    • Winkelmann, D. A., Lowey, S., and Press, J. L. (1983) Monoclonal antibodies localize changes on myosin heavy chain isozymes during avian myogenesis, Cell 34, 295-306.
    • (1983) Cell , vol.34 , pp. 295-306
    • Winkelmann, D.A.1    Lowey, S.2    Press, J.L.3
  • 41
    • 0022658288 scopus 로고
    • Difference between subfragment-1 and heavy meromyosin in their interaction with F-actin
    • Yamamoto, K., and Sekine, T. (1986) Difference between subfragment-1 and heavy meromyosin in their interaction with F-actin, J. Biochem. 99, 199-206.
    • (1986) J. Biochem. , vol.99 , pp. 199-206
    • Yamamoto, K.1    Sekine, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.