Interaction of myosin with F-actin: Time-dependent changes at the interface are not slow

Biophysical Journal

Volumn 78, Issue 6, 2000, Pages 3093-3102

  Van Dijk, Juliette ^a   Céline, Fernandez ^a   Barman, Tom ^b   Chaussepied, Patrick ^a  

^a Centre National de la Recherche Scientifique   (France)

^b INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM); ADENOSINE TRIPHOSPHATE; CYANAMIDE; F ACTIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

ACTIN FILAMENT; ACTIN MYOSIN INTERACTION; ANIMAL TISSUE; ARTICLE; CROSS LINKING; ENZYME ACTIVITY; NONHUMAN; RABBIT;

EID: 0342657210     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76846-9     Document Type: Article

References (70)

1. Amos, L. A., H. E. Huxley, K. C. Holmes, R. S. Goody, and K. A. Taylor. 1982. Structural evidence that myosin heads may interact with two sites on F-actin. Nature. 299:467-469.
2. Ando, T., and D. Scales. 1985. Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments. J. Biol. Chem. 260: 2321-2327.
3. Andreev, O. A., A. L. Andreeva, and J. Borejdo. 1993a. Polarization of fluorescently labeled myosin subfragment-1 fully or partially decorating muscle fibers and myofibrils. Biophys. J. 65:1027-1038.
4. Andreev, O. A., A. L. Andreeva, V. S. Markin, and J. Borejdo. 1993b. Two different rigor complexes of myosin subfragment 1 and actin. Biochemistry 32:12046-12053.
5. Andreev, O. A., and J. Borejdo. 1991. The myosin head can bind two actin monomers. Biochem. Biophys. Res. Commun. 177:350-356.
6. Andreev, O. A., and J. Borejdo. 1992a. Binding of myosin subfragment-1 to F-actin. Biochem. Biophys. Res. Commun. 188:94-101.
7. Andreev, O. A., and J. Borejdo. 1992b. Two different acto-S1 complexes. J. Muscle Res. Cell Motil. 13:523-533.
8. Andreev, O. A., and J. Borejdo. 1995. Binding of heavy-chain and essential light-chain 1 of S1 to actin depends on the degree of saturation of F-actin filaments with S1. Biochemistry. 34:14829-14833.
9. Andreev, O. A., and J. Borejdo. 1997. Interaction of the heavy and light chains of cardiac myosin subfragment-1 with F-actin. Circ. Res. 81: 688-693.
10. Andreev, O. A., L. D. Saraswat, S. Lowey, C. Slaughter, and J. Borejdo. 1999. Interaction of the N-terminus of chicken skeletal essential light chain 1 with F-actin. Biochemistry. 38:2480-2485.
11. Andreev, O. A., R. Takashi, and J. Borejdo. 1995. Fluorescence polarization study of the rigor complexes formed at different degrees of saturation of actin filaments with myosin subfragment-1. J. Muscle Res. Cell Motil. 16:353-367.
12. Andreev, O. A., D. S. Ushakov, and J. Borejdo. 1998. Effect of ADP on binding of skeletal S1 to F-actin. Biochemistry. 37:17836-17842.
13. Andreeva, A. L., O. A. Andreev, and J. Borejdo. 1993. Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin. Biochemistry. 32:13956-13960.
14. Barman, T. E., and F. Travers. 1985. The rapid-flow-quench method in the study of fast reactions in biochemistry: extension to subzero conditions. Methods Biochem. Anal. 31:1-59.
15. 2-terminal segment of residues 1-28. Eur. J. Biochem. 181:747-754.
16. Blanchoin, L., D. Didry, M. F. Carlier, and D. Pantaloni. 1996. Kinetics of association of myosin subfragment-1 to unlabeled and pyrenyl-labeled actin. J. Biol. Chem. 271:12380-12386.
17. Blotnick, E., C. Miller, U. Groschel-Stewart, and A. Muhlrad. 1995. Immunochemical probing of the functional role of the 238-246 and 567-574 sequences of myosin heavy chain. Eur. J. Biochem. 232: 235-240.
18. Boey, W., A. W. Everett, J. Sleep, J. Kendrick-Jones, and R. C. dos Remedios. 1992. Uncoupling of actin-activated myosin ATPase activity from actin binding by a monoclonal antibody directed against the N-terminus of myosin light chain 1. Biochemistry. 31:4090-4095.
19. Bonafe, N., and P. Chaussepied. 1995. A single myosin head can be cross-linked to the N termini of two adjacent actin monomers. Biophys. J. 68:35S-43S.
20. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
21. Carlier, M. F., D. Didry, and C. Valentin-Ranc. 1991. Interaction between chromium GTP and tubulin. Stereochemistry of GTP binding, GTP hydrolysis, and microtubule stabilization. J. Biol. Chem. 266: 12361-12368.
22. Chaussepied, P., and J. Van Dijk. 1999. Role of charges in actomyosin interactions. In Molecular Interactions of Actin. Springer-Verlag, Berlin and New York.
23. Chen, T., D. Applegate, and E. Reisler. 1985. Cross-linking of actin to myosin subfragment 1 in the presence of nucleotides. Biochemistry. 24:5620-5625.
24. Cheung, P., and E. Reisler. 1992. Synthetic peptide of the sequence 632-642 on myosin subfragment 1 inhibits actomyosin ATPase activity. Biochem. Biophys. Res. Commun. 189:1143-1149.
25. Combeau, C., D. Didry, and M. F. Carlier. 1992. Interaction between G-actin and myosin subfragment-1 probed by covalent cross-linking. J. Biol. Chem. 267:14038-14046.
26. Cooke, R. 1986. The mechanism of muscle contraction. CRC Crit. Rev. Biochem. 21:53-118.
27. Cooper, J. A., S. B. Walker, and T. D. Pollard. 1983. Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. Cell Motil. 4:253-262.
28. Criddle, A. H., M. A. Geeves, and T. Jeffries. 1985. The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem. J. 232:343-349.
29. Eisenberg, E., and W. W. Kielley. 1974. Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present. J. Biol. Chem. 249:4742-4748.
30. Elzinga, M. 1986. Carboxyl group reactivity in actin. In Methods in Protein Science Analysis. K. E. Walsh, editor. The Human Press. 615-623.
31. Geeves, M. A. 1989. Dynamic interaction between actin and myosin subfragment 1 in the presence of ADP. Biochemistry. 28:5864-5871.
32. Geeves, M. A., and P. B. Conibear. 1995. The role of three-state docking of myosin S1 with actin in force generation. Biophys. J. 68:194S-199S.
33. Grabarek, Z., and J. Gergely. 1990. Zero-length crosslinking procedure with the use of active esters. Anal. Biochem. 185:131-135.
34. Greene, L. E., and E. Eisenberg. 1980. The binding of heavy meromyosin to F-actin. J. Biol. Chem. 255:549-554.
35. Herrmann, C., J. Sleep, P. Chaussepied, F. Travers, and T. Barman. 1993. A structural and kinetic study on myofibrils prevented from shortening by chemical cross-linking. Biochemistry. 32:7255-7263.
36. Hibberd, M. G., M. R. Webb, Y. E. Goldman, and D. R. Trentham. 1985. Oxygen exchange between phosphate and water accompanies calcium-regulated ATPase activity of skinned fibers from rabbit skeletal muscle. J. Biol. Chem. 260:3496-3500.
37. Holmes, K. C., D. Popp, W. Gebhard, and W. Kabsch. 1990. Atomic model of the actin filament. Nature. 347:44-49.
38. Huxley, H. E. 1969. The mechanism of muscular contraction. Science. 164:1356-1366.
39. Kouyama, T., and K. Mihashi. 1981. Fluorimetry study of N-(1-pyrenyl)iodoacelamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114:33-38.
40. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
41. Lheureux, K., T. Forne, and P. Chaussepied. 1993. Interaction and polymerization of the G-actin-myosin head complex: effect of DNase I. Biochemistry. 32:10005-10014.
42. Lowey, S., G. S. Waller, and K. M. Trybus. 1993. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature. 365:454-456.
43. Lymn, R. W., and E. W. Taylor. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 10:4617-4624.
44. Miller, C. J., P. Cheung, P. White, and E. Reisler. 1995. Actin's view of actomyosin interface. Biophys. J. 68:50S-54S.
45. Milligan, R. A. 1996. Protein-protein interactions in the rigor actomyosin complex. Proc. Natl. Acad. Sci. USA. 93:21-26.
46. Mornet, D., R. Bertrand, P. Pantel, E. Audemard, and R. Kassab. 1981. Structure of the actin-myosin interface. Nature. 292:301-306.
47. Nikolaeva, O. P., N. L. Golitsina, D. I. Levitsky, L. N. Moiseeva, and B. I. Kurganov. 1994. Kinetics of interaction of myosin subfragment 1 isoforms with F-actin. Biochem. Mol. Biol. Int. 33:553-560.
48. Offer, G., C. Moos, and R. Starr. 1973. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterisation. J. Mol. Biol. 74:653-676.
49. Panusz, H. T., G. Graczyk, D. Wilmanska, and J. Skarzynski. 1970. Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities. Anal. Biochem. 35:494-504.
50. Prince, H. P., H. R. Trayer, G. D. Henry, I. P. Trayer, D. C. Dalgarno, B. A. Levine, P. D. Cary, and C. Turner. 1981. Proton nuclear-magnetic-resonance spectroscopy of myosin subfragment 1 isoenzymes. Eur. J. Biochem. 121:213-219.
51. Rayment, I., H. M. Holden, M. Whittaker, C. B. Yohn, M. Lorenz, K. C. Holmes, and R. A. Milligan. 1993. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 261:58-65.
52. Schoenberg, M. 1988. The kinetics of weakly and strongly binding cross-bridges: implications for contraction and relaxation. Adv. Exp. Med. Biol. 226:189-202.
53. Schroder, R. R., D. J. Manstein, W. Jahn, H. Holden, I. Rayment, K. C. Holmes, and J. A. Spudich. 1993. Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature. 364:171-174.
54. Spudich, J. A. 1994. How molecular motors work. Nature. 372:515-518.
55. Sutoh, K. 1982. Identification of myosin-binding sites on the actin sequence. Biochemistry. 21:3654-3661.
56. Sutoh, K. 1983. Mapping of actin-binding sites on the heavy chain of myosin subfragment 1. Biochemistry. 22:1579-1585.
57. Taylor, E. W. 1991. Kinetic studies on the association and dissociation of myosin subfragment 1 and actin. J. Biol. Chem. 266:294-302.
58. Tesi, C., F. Travers, and T. Barman. 1990. Cryoenzymatic studies on actomyosin ATPase. Evidence that the degree of saturation of actin with S1 affects the kinetics of the binding of ATP. Biochemistry. 29: 1846-1852.
59. Timson, D. J., and I. P. Trayer. 1997. The role of the proline-rich region in A1-type myosin essential light chains: implications for information transmission in the actomyosin complex. FEBS Lett. 400:31-36.
60. Timson, D. J., H. R. Trayer, and I. P. Trayer. 1998. The N-terminus of A1-type myosin essential light chains binds actin and modulates myosin motor function. Ear. J. Biochem. 255:654-662.
61. Trayer, I. P., H. R. Trayer, and B. A. Levine. 1987. Evidence that the N-terminal region of Al-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study. Eur. J. Biochem. 164:259-266.
62. Van Dijk, J., C. Fernandez, and P. Chaussepied. 1998. Effect of ATP analogues on the actin-myosin interface. Biochemistry. 37:8385-8394.
63. Van Dijk, J., M. Furch, J. Derancourt, R. Batra, M. L. Knetsch, D. J. Manstein, and P. Chaussepied. 1999a. Differences in the ionic interaction of actin with the motor domains of nonmuscle and muscle myosin II. Eur. J. Biochem. 260:672-683.
64. Van Dijk, J., M. Furch, C. Lafont, D. Manstein, and P. Chaussepied. 1999b. Functional characterization of the secondary actin binding site of myosin II. Biochemistry. (in press).
65. Weeds, A. G., and R. S. Taylor. 1975. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature. 257:54-56.
66. White, H. D., and E. W. Taylor. 1976. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry, 15:5818-5826.
67. Winstanley, M. A., D. A. Small, and I. P. Trayer. 1979. Differential binding of myosin subfragment one species to immobilized ADP and actin: the influence of the alkali light chains. Eur. J. Biochem. 98: 441-446.
68. Yamamoto, K. 1989. Binding manner of actin to the lysine-rich sequence of myosin subfragment 1 in the presence and absence of ATP. Biochemistry. 28:5573-5577.
69. Yamamoto, K. 1990. Shift of binding site at the interface between actin and myosin. Biochemistry. 29:844-848.
70. Yamamoto, K., and T. Sekine. 1983. Interaction of alkali light chain 1 with actin: effect of ionic strength on the cross-linking of alkali light chain 1 with actin. J. Biochem. (Tokyo). 94:2075-2078.