Novel Mode of Cooperative Binding between Myosin and Mg2+-actin Filaments in the Presence of Low Concentrations of ATP

Journal of Molecular Biology

Volumn 386, Issue 1, 2009, Pages 149-162

  Tokuraku, Kiyotaka ^a,b   Kurogi, Rika ^a   Toya, Ryo ^a   Uyeda, Taro Q P ^b  

^a MIYAKONOJO NATIONAL COLLEGE OF TECHNOLOGY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

actin; ATP; cooperative binding; heavy meromyosin; myosin

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CALCIUM; MAGNESIUM; MEROMYOSIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; PHALLOIDIN;

ACTIN FILAMENT; ANIMAL TISSUE; ARTICLE; DICTYOSTELIUM; FLUORESCENCE MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; QUANTITATIVE ANALYSIS; SKELETAL MUSCLE; STOICHIOMETRY;

DICTYOSTELIUM; ORYCTOLAGUS CUNICULUS;

EID: 58549113967     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.12.008     Document Type: Article

References (35)

1. Alberts B., Johnson A., Lewis J., Raff M., Roberts K., and Walter P. Molecular biology of the Cell. 4th edit. (2002), Garland Science, New York
2. Oosawa F. Macromolecular assembly of actin. In: Stracher A. (Ed). Muscle and Non-muscle Motility (1983), Academic Press, New York 151-216
3. Egelman E.H., and Orlova A. New insights into actin filament dynamics. Curr. Opin. Struct. Biol. 5 (1995) 172-180
4. Oosawa F., Fujime S., Ishiwata S., and Mihashi K. Dynamic property of F-actin and thin filament. Cold Spring Harbor Symp. Quant. Biol. 37 (1972) 277-285
5. Tawada K. Physicochemical studies of F-actin-heavy meromyosin solutions. Biochim. Biophys. Acta 172 (1969) 311-318
6. Fujime S., and Ishiwata S. Dynamic study of F-actin by quasielastic scattering of laser light. J. Mol. Biol. 62 (1971) 251-265
7. Loscalzo J., Reed G.H., and Weber A. Conformational change and cooperativity in actin filaments free of tropomyosin. Proc. Natl Acad. Sci. USA 72 (1975) 3412-3415
8. Thomas D.D., Seidel J.C., and Gergely J. Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range. J. Mol. Biol. 132 (1979) 257-273
9. Miki M., Wahl P., and Auchet J.C. Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads. Biochemistry 21 (1982) 3661-3665
10. Woodrum D.T., Rich S.A., and Pollard T.D. Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method. J. Cell Biol. 67 (1975) 231-237
11. 2+-regulated myosin. J. Mol. Biol. 140 (1980) 35-55
12. Frado L.L., and Craig R. Electron microscopy of the actin-myosin head complex in the presence of ATP. J. Mol. Biol. 223 (1992) 391-397
13. Walker M., White H., Belknap B., and Trinick J. Electron cryomicroscopy of acto-myosin-S1 during steady-state ATP hydrolysis. Biophys. J. 66 (1994) 1563-1572
14. Orlova A., and Egelman E.H. Cooperative rigor binding of myosin to actin is a function of F-actin structure. J. Mol. Biol. 265 (1997) 469-474
15. Vilfan A., Frey E., Schwabl F., Thormahlen M., Song Y.H., and Mandelkow E. Dynamics and cooperativity of microtubule decoration by the motor protein kinesin. J. Mol. Biol. 312 (2001) 1011-1026
16. Wendt T.G., Volkmann N., Skiniotis G., Goldie K.N., Muller J., Mandelkow E., and Hoenger A. Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncd. EMBO J. 21 (2002) 5969-5978
17. Muto E., Sakai H., and Kaseda K. Long-range cooperative binding of kinesin to a microtubule in the presence of ATP. J. Cell Biol. 168 (2005) 691-696
18. Siddique M.S., Mogami G., Miyazaki T., Katayama E., Uyeda T.Q.P., and Suzuki M. Cooperative structural change of actin filaments interacting with activated myosin motor domain, detected with copolymers of pyrene-labeled actin and acto-S1 chimera protein. Biochem. Biophys. Res. Commun. 337 (2005) 1185-1191
19. Kozuka J., Yokota H., Arai Y., Ishii Y., and Yanagida T. Dynamic polymorphism of single actin molecules in the actin filament. Nature Chem. Biol. 2 (2006) 83-86
20. Kunioka Y., and Ando T. Innocuous labeling of the subfragment-2 region of skeletal muscle heavy meromyosin with a fluorescent polyacrylamide nanobead and visualization of individual heavy meromyosin molecules. J. Biochem. (Tokyo) 119 (1996) 1024-1032
21. Kitazawa T., Shuman H., and Somlyo A.P. Calcium and magnesium binding to thin and thick filaments in skinned muscle fibres: electron probe analysis. J. Muscle Res. Cell Motil. 3 (1982) 437-454
22. Greene L.E. Comparison of the equilibrium binding of heavy meromyosin and myosin to F-actin in the presence and absence of the troponin-tropomyosin complex. FEBS Lett. 139 (1982) 233-236
23. Uyeda T.Q.P., Tokuraku K., Kaseda K., Webb M.R., and Patterson B. Evidence for a novel, strongly bound acto-S1 complex carrying ADP and phosphate stabilized in the G680V mutant of Dictyostelium myosin II. Biochemistry 41 (2002) 9525-9534
24. Batra R., Geeves M.A., and Manstein D.J. Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region. Biochemistry 38 (1999) 6126-6134
25. Goodno C.C. Inhibition of myosin ATPase by vanadate ion. Proc. Natl Acad. Sci. USA 76 (1979) 2620-2624
26. Tokuraku K., and Uyeda T.Q.P. Phalloidin affects the myosin-dependent sliding velocities of actin filaments in a bound-divalent cation dependent manner. J. Muscle Res. Cell Motil. 22 (2001) 371-378
27. Kitamura K., Tokunaga M., Iwane A.H., and Yanagida T. A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature 397 (1999) 129-134
28. Tanaka H., Homma K., Iwane A.H., Katayama E., Ikebe R., Saito J., et al. The motor domain determines the large step of myosin-V. Nature 415 (2002) 192-195
29. Pardee J.D., and Spudich J.A. Purification of muscle actin. Methods Enzymol. 85 (1982) 164-181
30. Hynes T.R., Block S.M., White B.T., and Spudich J.A. Movement of myosin fragments in vitro: domains involved in force production. Cell 48 (1987) 953-963
31. Okamoto Y., and Sekine T. A streamlined method of subfragment one preparation from myosin. J. Biochem. (Tokyo) 98 (1985) 1143-1145
32. Ruppel K.M., Uyeda T.Q.P., and Spudich J.A. Role of highly conserved lysine 130 of myosin motor domain. In vivo and in vitro characterization of site specifically mutated myosin. J. Biol. Chem. 269 (1994) 18773-18780
33. Egelhoff T.T., Titus M.A., Manstein D.J., Ruppel K.M., and Spudich J.A. Molecular genetic tools for study of the cytoskeleton in Dictyostelium. Methods Enzymol. 196 (1991) 319-334
34. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
35. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685