Abstract
Actin was discovered by F. B. Straub more than 50 years ago as one of the main components of muscle proteins and as a partner of myosin for superprecipitation coupled with the hydrolysis of ATP (Straub 1942). When extracted from dried muscle powder into water, actin was in the state of dispersed monomers, named G-actin, and transformed to fibrous polymers, named F-actin, in a solution of neutral salts. With removal of salts, F-actin returned to G-actin. Later, he noticed that this G-F transformation was coupled with the hydrolysis of ATP bound to G-actin; ADP produced were kept bound to F-actin (Straub and Feuer 1950). The reverse transformation from F to G was not associated with rephosphorylation of bound ADP; G-actin released ADP and bound new ATP in solution.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Asakura S, Oosawa F (1960) Dephosphorylation of ATP in actin solutions at low concentration of Mg ions. Arch Biochem Biophys 87: 273–285
Asakura S, Kasai M, Oosawa F (1960) The effect of temperature on the equilibrium state of actin solutions. J Polym Sci 44: 35–49
Asakura S, Taniguchi M, Oosawa F (1963) Mechanochemical behavior of F-actin. J Mol Biol 7: 55–69
Carlier M-F (1990) Actin polymerization and ATP hydrolysis. Adv Biophys 26: 51–73
Carlier M-F, Pantaloni D, Korn E (1984) Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state. J Biol Chem 259: 9983–9986
Ebashi S, Endo M (1968) Calcium ions and muscle contraction. Prog Biophys Mol Biol 18: 123–183
Faucheux L, Bourdieu L, Kaplan P, Libchaber A (1995) Optical thermal ratchet. Phys Rev Lett 74: 1504–1507
Finer J, Simmons R, Spudich JA (1994) Single myosin molecule mechanics; picoNewton forces and nanometer steps. Nature 369: 113–119
Fujime S (1970) Quasielastic light scattering from solutions of macromolecules, II Doppler broadening of light scattered from solutions of semi-flexible polymers, F-actin. J Phys Soc Jpn 29: 751–759
Funatsu T, Harada Y, Tokunaga M, Saito K, Yanagida T (1995) Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374: 555–559
Hanson J, Lowy J (1963) The structure of F-actin and actin filaments isolated from muscle. J Mol Biol 6: 46–60
Harada Y, Sakurada K, Aoki T, Thomas DD, Yanagida T (1990) Mechanochemical coupling in actomyosin energy transduction studied by in vitro motility assay. J Mol Biol 216: 49–68
Hatano S (1994) Actin-binding proteins in cell motility. Int Rev Cytol 156: 199–273
Hatano S, Oosawa F (1966) Isolation and characterization of plasmodium actin. Biochim Biophys Acta 127: 488–498
Hatano S, Totsuka T, Oosawa F (1967) Polymerization of plasmodium actin. Biochim Biophys Acta 140: 109–122
Higashi-Fujime S (1980) Active movement in vitro of bundles of microfilaments isolated from Nitella cell. J Cell Biol 87: 569–578
Holmes K, Popp D, Gebhard W, Kabsch W (1990) Atomic model of the actin filament. Nature 347: 44–49
Huxley AF (1998) Biological motors: Energy storage in myosin molecules. Curr Biol 8: 485–488
Huxley AF, Niedergerke R (1954) Structural changes in muscle during contraction. Nature 173: 971–973
Huxley H, Stewart A, Sosa H, Irving T (1994) X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys J 67: 2411–2421
Huxley HE (1963) Electronmicroscopic studies on the structure of natural and synthetic protein filaments from striated muscle. J Mol Biol 7: 281–308
Huxley HE (1973) Cold Spring Harbor Symp. Quant Biol 37: 361–376
Huxley HE, Hanson J (1954) Changes in the cross-striation of muscle during contraction and stretch and their structural interpretation. Nature 173: 973–975
Ishijima A, Harada Y, Kojima H, Funatsu T, Higuchi H, Yanagida T (1994) Single molecule analysis of the actomyosin motor using nano-manipulation. Biochem Biophys Res Commun 199: 1057–1063
Ishijima A, Kojima H, Funatsu T, Tokunaga M, Higuchi H, Tanaka H, Yanagida T (1998) Simultaneous observation of individual Atpase and mechanical events by a single myosin molecule during interaction with actin. Cell 92: 161–171
Ishiwata S, Fujime S (1972) Effect of calcium ions on the flexibility of reconstituted thin filament of muscle studied by quasielastic light scattering of laser light. J Mol Biol 68: 511–522
Kabsch W, Mannherz H, Suck D, Pai E, Holmes K (1990) Atomic structure of the actin-DNase Icomplex. Nature 347: 37–43
Kamiya N, Kuroda K (1956) Velocity distribution of protoplasmic streaming in Nitella cells. Bot Mag 69: 544–554
Kasai M, Asakura S, Oosawa F (1962) Cooperative nature of G-F transformation of actin. Biochim Biophys Acta 57: 22–31
Kasai M, Nakano E, Oosawa F (1965) Polymerization of actin free from nucleotides and divalent cations. Biochim Biophys Acta 94: 494–503
Kishino A, Yanagida T (1988) Force measurements by micromanipulation of a single actin filament by glass needle. Nature 334: 74–76
Kitamura K, Tokunaga M, Iwane A, Yanagida T (1999) A single myosin head moves along an actin filament with regular steps of 5.3 nm. Nature 397: 129–134
Kojima H, Ishijima A, Yanagida T (1994) Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc Natl Acad Sci USA 91: 12962–12966
Kondo H, Ishiwata S (1976) Unidirectional growth of F-actin. J Biochem 79: 159–171
Kron S, Spudich JA (1986) Fluorescent actin filaments move on myosin fixed on a glass surface. Proc Natl Acad Sci USA 83: 6272–6276
Magnesco M (1993) Forced thermal ratchet. Phys Rev Lett 71: 1477–1481
Nagashima H, Asakura S (1980) Dark field light microscopic study of the flexibility of F-actin complexes. J Mol Biol 136: 169–182
Oosawa F, Asakura S (1975) Thermodynamics of the polymerization of protein. Academic Press New York
Oosawa F, Hayashi S (1986) The loose coupling mechanism in molecular machines of living cells. Adv Biophys 22: 151–183
Oosawa F, Kasai M (1962) Theory of linear and helical polymerization of macromolecules. J Mol Biol 4: 10–21
Oosawa F, Asakura S, Ooi T (1961) Physical chemistry of muscle protein, actin. Prog Theor Phys suppl 17: 14–34
Oosawa F, Asakura S, Hotta K, Imai N, Ooi T (1959) G-F transformation of actin as a fibrous condensation. J Polym Sci 37: 323–336
Oosawa F, Fujime S, Ishiwata S, Mihashi K (1973) Dynamic property of F-actin and thin filament. Cold Spring Harbor Symp Quant Biol 37: 277–286
Oosawa F (1983) Macromolecular assembly of actin In: Stracher A (ed)., Muscle nonmuscle motility, Academic Press New York, 152–216
Oosawa F (1993) Physical chemistry of actin: past, present and future. Biophys Chem 47: 101–111
Oosawa F (1995) Sliding and ATPase. J Biochem 118: 863–870
Orlova A, Egelman E (1995) Structural dynamics of F-actin I. J Mol Biol 245: 582–597
Orlova A, Prochniewicz E, Egelman EH (1995) Structural dynamics of F-actin II. J Mol Biol 245: 598–607
Straub FB, Feuer G (1950) Adenosinetriphosphate, the functional group of actin. Biochim Biophys Acta 4: 455–470
Straub FB (1942) Actin. Studies Med Inst Szeged 2: 3–15
Szent-Györgyi A (1951) Chemistry of muscular contraction Academic Press, New York
Takebayashi T, Morita Y, Oosawa F (1977) Electronmicroscopic investigation of the flexibility of F-actin. Biochim Biophys Acta 492: 357–363
Tilney L, DeRosier D, Tilney M (1992) How Listeria exploits host cell actin to form its own cytoskeleton. J Cell Biol 118: 71–81
Vale R, Oosawa F (1990) Protein motors and Maxwell’s demons: Does mechanochemical transduction involve a thermal ratchet? Adv Biophys 26: 97–131
Wakabayashi K, Sugimoto Y, Tanaka H, Ueno Y, Takezawa Y, Amemiya Y (1994) X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys J 67: 2422–2435
Yanagida T, Nakase M, Nishiyama N, Oosawa F (1984) Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307: 58–60
Yanagida T, Arata T, Oosawa F (1985) Sliding distance of actin filament induced by a myosin cross-bridge during one ATP hydrolysis cycle. Nature 316: 366–369
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Oosawa, F. (2001). A Historical Perspective of Actin Assembly and Its Interactions. In: dos Remedios, C.G., Thomas, D.D. (eds) Molecular Interactions of Actin. Results and Problems in Cell Differentiation, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46560-7_2
Download citation
DOI: https://doi.org/10.1007/978-3-540-46560-7_2
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-53675-5
Online ISBN: 978-3-540-46560-7
eBook Packages: Springer Book Archive