메뉴 건너뛰기




Volumn 84, Issue 2 I, 2003, Pages 1047-1056

Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever-arm movement

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ADENOSINE TRIPHOSPHATASE; F ACTIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; TRINITROPHENYL;

EID: 0037306093     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74921-2     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 0033580652 scopus 로고    scopus 로고
    • Trinitrophenylated reactive lysine residue in myosin detects lever arm movement during the consecutive steps of ATP hydrolysis
    • Ajtai, K., Y. M. Peyser, S. Park, T. P. Burghardt, and A. Muhlrad. 1999. Trinitrophenylated reactive lysine residue in myosin detects lever arm movement during the consecutive steps of ATP hydrolysis. Biochemistry. 38:6428-6440.
    • (1999) Biochemistry , vol.38 , pp. 6428-6440
    • Ajtai, K.1    Peyser, Y.M.2    Park, S.3    Burghardt, T.P.4    Muhlrad, A.5
  • 2
    • 0016233229 scopus 로고
    • The characterization of myosin-product complexes and product-release steps during the magnesium ion-dependent adenosine triphosphate reaction
    • Bagshaw, C. R., and D. R. Trentham. 1974. The characterization of myosin-product complexes and product-release steps during the magnesium ion-dependent adenosine triphosphate reaction. Biochem. J. 141:331-349.
    • (1974) Biochem. J. , vol.141 , pp. 331-349
    • Bagshaw, C.R.1    Trentham, D.R.2
  • 3
    • 0002230535 scopus 로고
    • Conformational energy estimates for statistically coiling polypeptide chains
    • Brant, D. A., W. G. Miller, and P. J. Flory. 1967. Conformational energy estimates for statistically coiling polypeptide chains. J. Mol. Biol. 23:47-65.
    • (1967) J. Mol. Biol. , vol.23 , pp. 47-65
    • Brant, D.A.1    Miller, W.G.2    Flory, P.J.3
  • 4
    • 0022295424 scopus 로고
    • Fraction of myosin cross-bridges bound to actin in active muscle fibers: Estimation by fluorescence anisotropy measurements
    • Burghardt, T. P., and K. Ajtai. 1985. Fraction of myosin cross-bridges bound to actin in active muscle fibers: estimation by fluorescence anisotropy measurements. Proc. Natl. Acad. Sci. USA. 82:8478-8482.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8478-8482
    • Burghardt, T.P.1    Ajtai, K.2
  • 5
    • 0035901520 scopus 로고    scopus 로고
    • Conformation of myosin interdomain interactions during contraction: Deductions from muscle fibers using polarized fluorescence
    • Burghardt, T. P., A. R. Cruz-Walker, S. Park, and K. Ajtai. 2001a. Conformation of myosin interdomain interactions during contraction: deductions from muscle fibers using polarized fluorescence. Biochemistry. 40:4821-4833.
    • (2001) Biochemistry , vol.40 , pp. 4821-4833
    • Burghardt, T.P.1    Cruz-Walker, A.R.2    Park, S.3    Ajtai, K.4
  • 6
    • 0035901489 scopus 로고    scopus 로고
    • Conformation of myosin interdomain interactions during contraction: Deductions from proteins in solution
    • Burghardt, T. P., S. Park, and K. Ajtai. 2001b. Conformation of myosin interdomain interactions during contraction: deductions from proteins in solution. Biochemistry. 40:4834-4843.
    • (2001) Biochemistry , vol.40 , pp. 4834-4843
    • Burghardt, T.P.1    Park, S.2    Ajtai, K.3
  • 7
    • 0030893622 scopus 로고    scopus 로고
    • In vitro actin filament sliding velocities produced by mixtures of different types of myosin
    • Cuda, G., E. Pate, R. Cooke, and J. R. Sellers. 1997. In vitro actin filament sliding velocities produced by mixtures of different types of myosin. Biophys. J. 72:1767-1779.
    • (1997) Biophys. J. , vol.72 , pp. 1767-1779
    • Cuda, G.1    Pate, E.2    Cooke, R.3    Sellers, J.R.4
  • 8
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez, R., Y. Freyzon, K. M. Trybus, and C. Cohen. 1998. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell. 94:559-571.
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 9
    • 0014431412 scopus 로고
    • Effect of trinitrophenylation on myosin ATPase
    • Fabian, F., and A. Muhlrad. 1968. Effect of trinitrophenylation on myosin ATPase. Biochim. Biophys. Acta. 162:596-603.
    • (1968) Biochim. Biophys. Acta , vol.162 , pp. 596-603
    • Fabian, F.1    Muhlrad, A.2
  • 11
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch, M., M. A. Geeves, and D. J. Manstein. 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
  • 12
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M. A., and K. C. Holmes. 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
  • 13
    • 1642340974 scopus 로고    scopus 로고
    • Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head
    • Houdusse, A., V. N. Kalabokis, D. Himmel, A. G. Szent-Gyorgyi, and C. Cohen. 1999. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell. 97:459-470.
    • (1999) Cell , vol.97 , pp. 459-470
    • Houdusse, A.1    Kalabokis, V.N.2    Himmel, D.3    Szent-Gyorgyi, A.G.4    Cohen, C.5
  • 15
    • 0019878618 scopus 로고
    • Reactive lysyl of myosin subfragment 1: Location on the 27K fragment and labeling properties
    • Hozumi, T., and A. Muhlrad. 1981. Reactive lysyl of myosin subfragment 1: location on the 27K fragment and labeling properties. Biochemistry. 20:2945-2950.
    • (1981) Biochemistry , vol.20 , pp. 2945-2950
    • Hozumi, T.1    Muhlrad, A.2
  • 16
    • 0012825957 scopus 로고
    • On the active site of myosin A-adenosine triphosphatase. II. Properties of the trinitrophenyl enzyme and the enzyme free from divalent cations
    • Kitagawa, S., J. Yoshimura, and Y. Tonomura. 1961. On the active site of myosin A-adenosine triphosphatase. II. Properties of the trinitrophenyl enzyme and the enzyme free from divalent cations. J. Biol. Chem. 236:902-906.
    • (1961) J. Biol. Chem. , vol.236 , pp. 902-906
    • Kitagawa, S.1    Yoshimura, J.2    Tonomura, Y.3
  • 17
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green 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 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
  • 18
    • 0025826377 scopus 로고
    • The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain
    • Maita, T., E. Yajima, S. Nagata, T. Miyanishi, S. Nakayama, and G. Matsuda. 1991. The primary structure of skeletal muscle myosin heavy chain: IV. Sequence of the rod, and the complete 1,938-residue sequence of the heavy chain. J. Biochem. 110:75-87.
    • (1991) J. Biochem. , vol.110 , pp. 75-87
    • Maita, T.1    Yajima, E.2    Nagata, S.3    Miyanishi, T.4    Nakayama, S.5    Matsuda, G.6
  • 19
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian, S. S., and S. Lowey. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:55-72.
    • (1982) Methods Enzymol. , vol.85 , pp. 55-72
    • Margossian, S.S.1    Lowey, S.2
  • 20
    • 0033013185 scopus 로고    scopus 로고
    • Formation of the myosin.ADP.gallium fluoride complex and its solution structure by small-angle synchrotron X-ray scattering
    • Maruta, S., Y. Uyehara, K. Homma, Y. Sugimoto, and K. Wakabayashi. 1999. Formation of the myosin.ADP.gallium fluoride complex and its solution structure by small-angle synchrotron X-ray scattering. J. Biochem. 125:177-185.
    • (1999) J. Biochem. , vol.125 , pp. 177-185
    • Maruta, S.1    Uyehara, Y.2    Homma, K.3    Sugimoto, Y.4    Wakabayashi, K.5
  • 21
    • 0030449743 scopus 로고    scopus 로고
    • Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle
    • Miller, C. J., W. W. Wong, E. Bobkova, P. A. Rubinstein, and E. Reisler. 1996. Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry. 35:16557-16565.
    • (1996) Biochemistry , vol.35 , pp. 16557-16565
    • Miller, C.J.1    Wong, W.W.2    Bobkova, E.3    Rubinstein, P.A.4    Reisler, E.5
  • 22
    • 0018451581 scopus 로고
    • Differential modification of specific lysine residues in the two kinds of subfragments-1 of myosin with 2,4,6-trinitrobenzenesulfonate
    • Miyanishi, T., A. Inoue, and Y. Tonomura. 1979. Differential modification of specific lysine residues in the two kinds of subfragments-1 of myosin with 2,4,6-trinitrobenzenesulfonate. J. Biochem. 85:747-753.
    • (1979) J. Biochem. , vol.85 , pp. 747-753
    • Miyanishi, T.1    Inoue, A.2    Tonomura, Y.3
  • 24
    • 0020503223 scopus 로고
    • Mechanism of adenosinetriphosphatase activity of trinitrophenylated myosin subfragment 1
    • Muhlrad, A. 1983. Mechanism of adenosinetriphosphatase activity of trinitrophenylated myosin subfragment 1. Biochemistry. 22:3653-3660.
    • (1983) Biochemistry , vol.22 , pp. 3653-3660
    • Muhlrad, A.1
  • 25
    • 0014844770 scopus 로고
    • Effects of substrate and substrate analogues on the trinitrophenylation of myosin
    • Muhlrad, A., and F. Fabian. 1970. Effects of substrate and substrate analogues on the trinitrophenylation of myosin. Biochim. Biophys. Acta. 216:422-427.
    • (1970) Biochim. Biophys. Acta , vol.216 , pp. 422-427
    • Muhlrad, A.1    Fabian, F.2
  • 26
    • 0019887605 scopus 로고
    • Ionization of reactive lysyl residue of myosin subfragment 1
    • Muhlrad, A., and R. Takashi. 1981. Ionization of reactive lysyl residue of myosin subfragment 1. Biochemistry. 20:6749-6754.
    • (1981) Biochemistry , vol.20 , pp. 6749-6754
    • Muhlrad, A.1    Takashi, R.2
  • 27
    • 0001616942 scopus 로고
    • On the preparation and properties of 2,4,6-trinitrophenyl-amino acids and -peptides
    • Okuyama, T., and K. Satake. 1960. On the preparation and properties of 2,4,6-trinitrophenyl-amino acids and -peptides. J. Biochem. 47:454-462.
    • (1960) J. Biochem. , vol.47 , pp. 454-462
    • Okuyama, T.1    Satake, K.2
  • 28
    • 0003129925 scopus 로고
    • Inter- and intramolecular forces and molecular polarizability
    • I. Prigogine, editor. Interscience, New York
    • Pitzer, K. S. 1959. Inter- and intramolecular forces and molecular polarizability. In Advances in Chemical Physics. I. Prigogine, editor. Interscience, New York. 59-83.
    • (1959) Advances in Chemical Physics , pp. 59-83
    • Pitzer, K.S.1
  • 30
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(Il)ADP-vanadate complex of the dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith, C. A., and I. Rayment. 1996. X-ray structure of the magnesium(Il)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
  • 31
    • 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
  • 32
    • 0013877728 scopus 로고
    • On the molecular weight of myosin II
    • Tonomura, Y., P. Appel, and M. Morales. 1966. On the molecular weight of myosin II. Biochemistry. 5:515-521.
    • (1966) Biochemistry , vol.5 , pp. 515-521
    • Tonomura, Y.1    Appel, P.2    Morales, M.3
  • 33
    • 0001504870 scopus 로고
    • On the active site of myosin A-adenosine triphosphatase. IV. Properties of binding of trinitrobenzenesulfonate and p-chloromercuribenzoate to myosin A
    • Tonomura, Y., J. Yoshimura, and T. Onishi. 1963. On the active site of myosin A-adenosine triphosphatase. IV. Properties of binding of trinitrobenzenesulfonate and p-chloromercuribenzoate to myosin A. Biochim. Biophys. Acta. 78:698-700.
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 698-700
    • Tonomura, Y.1    Yoshimura, J.2    Onishi, T.3
  • 35
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G., and R. S. Taylor. 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
  • 36
    • 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. A., J. F. Eccleston, and M. A. Geeves. 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. 30:422-430.
    • (1991) Biochemistry , vol.30 , pp. 422-430
    • Woodward, S.K.A.1    Eccleston, J.F.2    Geeves, M.A.3
  • 37
    • 0000821005 scopus 로고    scopus 로고
    • Myosin as a motor and a back door enzyme
    • Abstr.
    • Yount, R. G. 1997. Myosin as a motor and a back door enzyme. FASEB J. 11:A855 (Abstr.).
    • (1997) FASEB J. , vol.11
    • Yount, R.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.