Electron microscopic evidence for the myosin head lever arm mechanism in hydrated myosin filaments using the gas environmental chamber

Biochemical and Biophysical Research Communications

Volumn 405, Issue 4, 2011, Pages 651-656

  Minoda, Hiroki ^a,b   Okabe, Tatsuhiro ^a   Inayoshi, Yuhri ^a   Miyakawa, Takuya ^c   Miyauchi, Yumiko ^c   Tanokura, Masaru ^c   Katayama, Eisaku ^d   Wakabayashi, Takeyuki ^e   Akimoto, Tsuyoshi ^e   Sugi, Haruo ^e  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d UNIVERSITY OF TOKYO   (Japan)

^e TEIKYO UNIVERSITY   (Japan)

Author keywords

Gas environmental chamber; Muscle contraction; Myosin filament; Myosin head; Transmission electron microscope

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; GOLD; MYOSIN;

ANALYTICAL EQUIPMENT; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; ELECTRON MICROSCOPY; GAS ENVIRONMENTAL CHAMBER; LIGHT CHAIN; MUSCLE CONTRACTION; MYOFILAMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING;

ADENOSINE TRIPHOSPHATE; ANIMALS; MICROSCOPY, ELECTRON; MUSCLE CONTRACTION; MYOSIN SUBFRAGMENTS; PROTEIN CONFORMATION; RABBITS;

EID: 79951957119     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.01.087     Document Type: Article

References (15)

1. Huxley A.F., Niedergerke R. Interference microscopy of living muscle fibres. Nature 1954, 173:971-973.
2. Huxley H.E., Hanson J. Changes in the cross striations of muscle during contraction and stretch. Nature 1954, 173:973-976.
3. Lymn R.W., Taylor E.W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 1971, 10:4617-4624.
4. Uyeda T.P.Q., Abramson P.D., Spudich J.A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl. Acad. Sci. USA 1996, 93:4459-4464.
5. Geeves M.A., Holmes K.C. Structural mechanism of muscle contraction. Ann. Rev. Biochem. 1999, 68:687-727.
6. Fisher S., Windschugel D., Horak D., Holmes K.C. Structural mechanism of the recovery stroke in the myosin molecular motor. Proc. Natl. Acad. Sci. USA 2005, 102:6873-6878.
7. Huxley H.E., Reconditi M, Stewertand A., et al. X-ray interference studies of cross-bridge action in muscle contraction: evidence from quick releases. J. Mol. Biol. 2006, 363:743-761.
8. Fukami A., Murakami S. Progress of electron microscopy of wet specimens using film-sealed environmental cell. J. Electron. Microsc. 1991, 28:S41.
9. Sugi H., Akimoto T., Sutoh K., et al. Dynamic electron microscopy of ATP-induced myosin head movement in living muscle thick filaments. Proc. Natl. Acad. Sci. USA 1997, 94:4378-4382.
10. Sugi H., Minoda H., Inayoshi Y., et al. Direct demonstration of the cross-bridge recovery stroke in muscle thick filaments in aqueous solution by using the hydration chamber. Proc. Natl. Acad. Sci. USA 2008, 105:17396-17401.
11. Sutoh K., Tokunaga M., Wakabayashi T. Electron microscopic mappings of myosin head with site-directed antibodies. J. Mol. Biol. 1989, 206:357-363.
12. Suda H., Ishikawa A., Fukami A. Evaluation of the critical electron dose on the contractile activity of hydrated muscle fibers in the film-sealed environmental cell. J. Electron Microsc. 1992, 41:223-229.
13. Muhlrad A., Peyser Y.M., Nili M., Ajtai K., et al. Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever-arm movement. Biophys. J. 2003, 84:1047-1056.
14. Milligan R.A. Protein-protein interactions in the rigor actomyosin complex. Proc. Natl. Acad. Sci. USA 1996, 93:21-26.
15. Kodera N., Yamamoto D., Ishikawa R., Ando T. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 2010, 468:72-76.