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Volumn 337, Issue 4, 2005, Pages 1185-1191

Cooperative structural change of actin filaments interacting with activated myosin motor domain, detected with copolymers of pyrene-labeled actin and acto-S1 chimera protein

Author keywords

Actin filament; Acto S1 chimera; Cooperative structural change; Dictyostelium; Fluorescence spectroscopy; Intermediate state; Motility function

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; COPOLYMER; MYOSIN; PYRENE;

EID: 27144435137     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.09.159     Document Type: Article
Times cited : (22)

References (25)
  • 2
    • 0034624066 scopus 로고    scopus 로고
    • X-Ray structures of the Apo and Mg-ATP-bound states of Dictyostelium discoideum myosin motor domain
    • C.B. Bauer, H.M. Holden, J.B. Thoden, R. Smith, and I. Rayment X-Ray structures of the Apo and Mg-ATP-bound states of Dictyostelium discoideum myosin motor domain J. Biol. Chem. 275 2000 38494 38499
    • (2000) J. Biol. Chem. , vol.275 , pp. 38494-38499
    • Bauer, C.B.1    Holden, H.M.2    Thoden, J.B.3    Smith, R.4    Rayment, I.5
  • 7
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • K.C. Holmes The swinging lever-arm hypothesis of muscle contraction Curr. Biol. 7 1997 112 118
    • (1997) Curr. Biol. , vol.7 , pp. 112-118
    • Holmes, K.C.1
  • 8
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • T.Q.P. Uyeda, P.D. Arramson, and J.A. Spudich The neck region of the myosin motor domain acts as a lever arm to generate movement Proc. Natl. Acad. Sci. USA 93 1996 4459 4464
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.P.1    Arramson, P.D.2    Spudich, J.A.3
  • 9
    • 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
    • C.J. Miller, W.W. Wong, E. Bobkova, P.A. Rubenstein, and E. Reisler 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 1996 16557 16565
    • (1996) Biochemistry , vol.35 , pp. 16557-16565
    • Miller, C.J.1    Wong, W.W.2    Bobkova, E.3    Rubenstein, P.A.4    Reisler, E.5
  • 10
    • 0037039297 scopus 로고    scopus 로고
    • Actin cross-linking and inhibition of the actomyosin motor
    • E. Kim, E. Bobkova, G. Hegyi, A. Muhlrad, and E. Reisler Actin cross-linking and inhibition of the actomyosin motor Biochemistry 41 2002 86 93
    • (2002) Biochemistry , vol.41 , pp. 86-93
    • Kim, E.1    Bobkova, E.2    Hegyi, G.3    Muhlrad, A.4    Reisler, E.5
  • 11
    • 0020364082 scopus 로고
    • Fluorescence anisotropy of labeled F actin: Influence of divalent cations on the interaction between F-actin and myosin heads
    • M. Miki, P. Wahl, and J.C. Auchet Fluorescence anisotropy of labeled F actin: influence of divalent cations on the interaction between F-actin and myosin heads Biochemistry 21 1982 3661 3665
    • (1982) Biochemistry , vol.21 , pp. 3661-3665
    • Miki, M.1    Wahl, P.2    Auchet, J.C.3
  • 13
    • 0017133794 scopus 로고
    • Fluorescence study of ε-ADP bound to rabbit F-actin: Structural change in the adenine subsite of F-actin under the influence of heavy meromyosin
    • M. Miki, T. Kouyama, and K. Mihashi Fluorescence study of ε-ADP bound to rabbit F-actin: structural change in the adenine subsite of F-actin under the influence of heavy meromyosin FEBS Lett. 66 1976 98 101
    • (1976) FEBS Lett. , vol.66 , pp. 98-101
    • Miki, M.1    Kouyama, T.2    Mihashi, K.3
  • 14
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • T. Kouyama, and K. Mihashi Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin Eur. J. Biochem. 114 1981 33 38
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 17
    • 0024837628 scopus 로고
    • The effects of various nucleotides on the structure of actin-attached myosin subfragment-1 studied by quick-freeze deep-etch electron microscopy
    • E. Katayama The effects of various nucleotides on the structure of actin-attached myosin subfragment-1 studied by quick-freeze deep-etch electron microscopy J. Biochem. (Tokyo) 106 1989 751 770
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 751-770
    • Katayama, E.1
  • 18
    • 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
    • T. Kodama, K. Fukui, and K. Kometani 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. (Tokyo) 99 1986 1465 1472
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 19
    • 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
    • J.A. Spudich, and S. Watt 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 1971 4866 4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 20
    • 0035747088 scopus 로고    scopus 로고
    • Solution properties of full length and truncated forms of myosin subfragment 1 from Dictyostelium discoideum
    • J.R. Reynoso Jr., A. Bobkov, A. Muhlrad, and E. Reisler Solution properties of full length and truncated forms of myosin subfragment 1 from Dictyostelium discoideum J. Muscle Res. Cell Motil. 22 2001 657 664
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 657-664
    • Reynoso Jr., J.R.1    Bobkov, A.2    Muhlrad, A.3    Reisler, E.4
  • 21
    • 0035951287 scopus 로고    scopus 로고
    • X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex
    • H. Iwamoto, K. Oiwa, T. Suzuki, and T. Fujisawa X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex J. Mol. Biol. 305 2001 863 874
    • (2001) J. Mol. Biol. , vol.305 , pp. 863-874
    • Iwamoto, H.1    Oiwa, K.2    Suzuki, T.3    Fujisawa, T.4
  • 22
    • 0022052149 scopus 로고
    • Thermodynamic analysis of muscle ATPase mechanisms
    • T. Kodama Thermodynamic analysis of muscle ATPase mechanisms Physiol. Rev. 65 1985 467 551
    • (1985) Physiol. Rev. , vol.65 , pp. 467-551
    • Kodama, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.