Imaging and nano-manipulation of single actomyosin motors at work

Clinical and Experimental Pharmacology and Physiology

Volumn 27, Issue 3, 2000, Pages 229-237

  Ishii, Yoshiharu ^a,d   Kimura, Yuji ^b   Kitamura, Kazuo ^a   Tanaka, Hiroto ^a   Wazawa, Tetsuichi ^a   Yanagida, Toshio ^a,b,c  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

^d Japan Science and Technology Agency   (Japan)

Author keywords

Actin; ATP hydrolysis; Fluorescence imaging; Fluorescence microscopy; Force production; Motility; Muscle contraction; Myosin; Protein; Single molecule

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

ACTIN MYOSIN INTERACTION; CONFERENCE PAPER; ENERGY METABOLISM; ENERGY RESOURCE; FLUORESCENCE SPECTROSCOPY; MOLECULAR INTERACTION; MUSCLE CONTRACTION; MUSCLE FORCE;

ACTOMYOSIN; ADENOSINE TRIPHOSPHATASES; ANIMALS; ENERGY METABOLISM; HUMANS; IMAGE PROCESSING, COMPUTER-ASSISTED; MUSCLE CONTRACTION; MUSCLE, SKELETAL;

EID: 0034059573     PISSN: 03051870     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1440-1681.2000.03226.x     Document Type: Conference Paper

References (36)

1. 1. Bagshaw CR. Muscle Contraction, 2nd edn. Chapman & Hall, London. 1984.
2. 2. Huxley AF, Niedergerke R, Structural changes in muscle during contraction. Nature 1954; 173: 971-3.
3. 3. Huxley HE, Hansen J. Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 1954; 173: 973-6.
4. 4. Yanagida T, Nakase M, Nishiyama K, Oosawa F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 1984; 307: 58-60.
5. 5. Kron SJ, Spudich JA. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl Acad. Sci. USA 1986; 83; 6272-6.
6. 6. Harada Y, Sakurada K, Aoki T, Yanagida T. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 1990; 216: 49-68.
7. 7. Funatsu T, Harada Y, Tokunaga M, Saito K, Yanagida T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 1995; 374: 555-9.
8. 8. Betzig E, Chichester RJ. Single molecules observed by near-field scanning optical microscope. Science 1993; 262: 1422-5.
9. 9. Vale RD, Funatsu T, Pierce DW, Romberg L, Harada Y, Yanagida T. Direct observation of single kinesin molecules moving along micro-tubules. Nature 1996; 380: 451-3.
10. 10. Tokunaga M, Kitamura K, Saito K, Iwane AH, Yanagida T. Single molecule imaging and enzymatic reactions achieved by objective-type total internal reflection microscopy. Biochem. Biophys. Res. Commun. 1997; 235: 47-53.
11. 11. Kishino A, Yanagida T. Force measurements by micromanipulation of a single actin filament by glass needles. Nature 1988; 334: 74-6.
12. 12. Ishijima A, Doi T, Sakurada K, Yanagida T. Sub-picoNewton force fluctuation of actomyosin in vitro. Nature 1991; 352: 301-6.
13. 13. Svoboda K, Schmidt CF, Schnapp BJ, Block SM. Direct observation of kinesin stepping by optical trapping interferometry. Nature 1993; 365: 721-7.
14. 14. Finer JT, Simmons RM, Spudich JA. Single myosin mechanics. PicoNewton forces and nanometre steps. Nature 1994; 368: 113-19.
15. 15. Molloy JE, Burns JE, Kendrick-Jones J, Tregear RT, White DCS. Movement and force produced by a single myosin head, Nature 1995; 378: 209-12.
16. 16. Ishijima A, Kojima H, Funatsu T, Tokunaga M, Higuchi H, Yanagida T, Simultaneous measurement of chemical and mechanical reaction. Cell 1998; 92: 161-71.
17. 17. Tanaka H, Ishijima A, Honda M, Saito K, Yanagida T. Orientation dependence of displacements by a single one-headed myosin relative to the actin filament. Biophys. J. 1998; 75: 1886-94.
18. 18. Iwane AH, Kitamura K, Tokunaga M, Yanagida T. Myosin subfragrnent-1 is fully equipped with factors essential for motor function. Biochem. Biophys. Res. Commun. 1997; 230: 76-80.
19. 19. Kitamura K, Tokunaga M, Iwane AH, Yanagida T. Myosin step size determined by directly manipulating a single S1 molecule with a scanning probe. Nature 1999; 397: 129-34.
20. 20. Huxley HE, The mechanism of muscular contraction. Science 1969; 164: 1356-66.
21. 21. Rayment I, Holden HM, Whittaker M et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 1993; 261: 58-65.
22. 22. Dominiquez R, Freyzon Y, Trybus KM, Cohen C. 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 1998; 94: 559-71.
23. 23. Lymn RW, Taylor EW. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 1971; 10: 4617-24.
24. 24. Eisenberg E, Hill TL, Chen Y. Cross-bridge model of muscle contraction: Quantitative analysis. Biophys. J. 1980; 29: 195-227.
25. 25. Frieden C. Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept, J. Biol. Chem. 1970; 245: 5788-99.
26. 26. Ishii Y, Yoshida T, Funatsu T, Wazawa T, Yanagida T. Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Physics 1999; 247: 163-73.
27. 27. Wazawa T, Ishii Y, Funatsu T, Yanagida T. Spectral fluctuation of a single fluorophore conjugated to a protein molecule. Biophys. J. 2000 (in press).
28. 28. Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 1978; 47: 819-46.
29. 29. Ishii Y, Funatsu T, Wazawa T et al. Communication between troponin-C and-I revealed by single molecule fluorescence spectroscopy and FRET. Biophys. J. 1997; 72: A283 (Abstract).
30. 30. Yokota H, Ishii Y, Wazawa T, Funatsu T, Yanagida T. Dynamic structure of single actin molecules revealed by FRET Imaging. Biophys. J. 1998; 74: A46 (Abstract).
31. 31. Lakowiczx JR, Gryczynski I, Cheung HC, Wang C-W, Johnson ML, Joshi N. Distance distribution in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C, Biochemistry 1988; 27: 9149-60.
32. 32. Wang Z, Mottonnen J, Goldsmith EJ. Kinetically controlled folding of the sperin plasminogen activator inhibitor 1. Biochemistry 1996; 35: 16443-8.
33. 33. Clark AC, Raso SW, Sinclair JF, Ziegler MM, Chaffotte AF, Baldwin T. Kinetic mechanism of luciferase subunit folding and assembly. Biochemistry 1997; 36: 1891-9.
34. 34. Sohl JL, Jaswal SS, Agard DA. Unfolded conformation of α-lytic protease are more stable than its native state. Nature 1998; 395: 817-19.
35. 35. Ito Y, Yamasaki K, Iwahara J et al. Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein. Biochemistry 1997; 36: 9109-19.
36. 36. Harrison PM, Bamborough P, Daggett V, Prusiner SB, Cohen FE, The prion folding problem. Curr. Opin. Struct. Biol. 1997; 7: 53-9.