Effect of the length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by X-ray fiber diffraction

Biophysical Journal

Volumn 75, Issue 6, 1998, Pages 2672-2681

  Oda, Toshiro ^a,c   Makino, Kouji ^a,b   Yamashita, Ichiro ^a   Namba, Keiichi ^a   Maéda, Yuichiro ^a  

^a PANASONIC CORPORATION   (Japan)

^b NAGOYA UNIVERSITY   (Japan)

^c ADVANCED TELECOMMUNICATIONS RESEARCH INSTITUTE INTERNATIONAL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; GELSOLIN; SODIUM CHLORIDE; SOLVENT;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; IONIC STRENGTH; LIQUID CRYSTAL; MUSCLE CELL; MYOFILAMENT; NONHUMAN; RABBIT; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0031795574     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77712-4     Document Type: Article

References (50)

1. Coppin, C. M., and P. C. Leavis. 1992. Quantitation of liquid-crystalline ordering in F-actin solutions. Biophys. J. 63:794-807.
2. Flory, P. J. 1956. Phase equilibria in solutions of rod-like particles. Proc. R. Soc. Lond. A. 234:73-89.
3. Fujime, S. 1970. Quasi-elastic 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.
4. Furukawa, R., R. Kundra, and M. Fechheimer. 1993. Formation of liquid crystals from actin filaments. Biochemistry. 32:12346-12352.
5. Garrels, J. I., and W. Gibson. 1976. Identification and characterization of multiple forms of actin. Cell 9:793-805.
6. Hanson, J., and S. Lowy. 1963. The structure of F-actin and of actin filaments isolated from muscle. J. Mol. Biol. 6:46-60.
7. Holmes, K. C. 1995. Solving the structure of macromolecular complexes with the help of x-ray fiber diffraction diagrams. J. Struct. Biol. 115: 151-158.
8. Holmes, K. C., and J. Barrington-Leigh. 1974. The effect of disorientation on the intensity distribution of non-crystalline fibers. I. Theory. Acta Crystallogr. A. 30:635-638.
9. Holmes, K. C., D. Popp, W. Gebhard, and W. Kabsch. 1990. Atomic model of the actin filament. Nature. 347:44-49.
10. Isambert, H., P. Venier, A. C. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M.-F. Carlier. 1995. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-11444.
11. Janmey, P. A., J. Peetermans, K. S. Zaner, T. P. Stossel, and T. Tanaka. 1986. Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry, and electron microscopy. J. Biol. Chem. 261:8357-8362.
12. Kabsch, W., H. G. Mannherz, D. Suck, E. F. Pai, and K. C. Holmes. 1990. Atomic structure of the actin:DNase I complex. Nature. 347:37-44.
13. Käs, J., H. Strey, J. X. Tang, D. Finger, R. Ezzell, E. Sackmann, and P. A. Janmey. 1996. F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions. Biophys. J. 70: 609-625.
14. Kawamura, M., and K. Maruyama. 1970a. Electron microscopic particle length of F-actin polymerized in vitro. J. Biochem. (Tokyo). 67: 437-457.
15. Kawamura, M., and K. Maruyama. 1970b. Polymorphism of F-actin. I. three forms of paracrystals. J. Biochem. (Tokyo). 68:885-899.
16. Kurokawa, H., W. Fujii, K. Ohmi, K. T. Sakurai, and Y. Nonomura. 1990. Simple and rapid purification of brevin. Biochem. Biophys. Res. Commun. 168:451-457.
17. Lednev, V. V., and D. Popp. 1990. Supercoiling of F-actin filaments. J. Struct. Biol. 103:225-231.
18. Lorenz, M., D. Popp, and K. Holmes. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
19. MacLean-Fletcher, S. D., and T. D. Pollard. 1980. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96:18-27.
20. Makowski, L. 1978. Processing of X-ray diffraction data from partially oriented specimens. J. Appl. Crystallogr. 11:273-283.
21. Makowski, L. 1991. An estimate of the number of structural parameters measurable from a fiber diffraction pattern. Acta Crystallogr. A. 47: 562-567.
22. Manning, G. S. 1978. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11:179-246.
23. Martonosi, A., C. M. Molino, and J. Gergely. 1964. The binding of divalent cations to actin. J. Biol. Chem. 239:1057-1064.
24. Matsudaira, P., E. Mandelkow, W. Renner, L. K. Hesterberg, and K. Weber. 1983. Role of fimbrin and villin in determining the interfilament distances of actin bundles. Nature. 301:209-214.
25. McLaughlin, P. J., J. T. Gooch, H. G. Mannherz, and A. G. Weeds. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 364:685-692.
26. Milligan, R. A., M. Whittaker, and D. Safer. 1990. Molecular structure of F-actin and location of surface binding sites. Nature. 348:217-221.
27. Nakajima, H., Y. Kunioka, K. Nakano, K. Shimizu, M. Seto, and T. Ando. 1997. Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin. Biochem. Biophys. Res. Commun. 234:178-182.
28. Nakamura, H., S. Nagashima, and T. Wakabayashi. 1994. Electrostatic field around the actin filament. In Synchrotron Radiation in the Biosciences. B. Chance, J. Deisenhofer, S. Ebashi, D. T. Goodhead, J. R. Helliwell, H. E. Huxley, T. Iizuka, J. Kirz, T. Mitsui, E. Rubenstein, N. Sakabe, T. Sasaki, G. Schmahl, H. B. Stuhrmann, K. Wüthrich, and G. Zaccai, editors. Clarendon Press, Oxford. 502-508.
29. Namba, K., R. Pattanayek, and G. Stubbs. 1989. Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 Å resolution by x-ray fiber diffraction. J. Mol. Biol. 208:307-325.
30. Namba, K., and G. Stubbs. 1985. Solving the phase problem in fiber diffraction. Application to tobacco mosaic virus at 3.6 Å resolution. Acta Crystallogr. A. 41:252-262.
31. Namba, K., and G. Stubbs. 1986. Structure of tobacco mosaic virus at 3.6 Å resolution: implications for assembly. Science. 231:1401-1406.
32. Odijk, T. 1985. Scaling theory of the isotropic-liquid crystalline phase transition in a solution of wormlike polymers. Polym. Commun. 26: 197-198.
33. Odijk, T. 1986. Theory of lyotropic polymer liquid crystals. Macromolecules. 19:2313-2329.
34. Onsager, L. 1949. The effects of shape on the interaction of colloidal particles. Ann. N.Y. Acad. Sci. 51:627-659.
35. Oosawa, F. 1971. Polyelectrolytes. Marcel Dekker, New York. 13-25.
36. Oosawa, F., and S. Asakura. 1975. Thermodynamics of the Polymerization of Protein. Academic Press, San Diego. 25-40.
37. Orlova, A., and E. H. Egelman. 1993. A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232:334-341.
38. Oster, G. 1950. Two-phase formation in solutions of tobacco mosaic virus and the problem of long-range forces. J. Gen. Physiol. 33:445-473.
39. Popp, D., V. V. Lednev, and W. Jahn. 1987. Methods of preparing well-orientated sols of F-actin containing filaments suitable for x-ray diffraction. J. Mol. Biol. 197:679-684.
40. Schutt, C. E., J. C. Myslik, M. D. Rozycki, N. C. W. Goonesekere, and U. Lindberg. 1993. The structure of crystalline profilin-β-actin. Nature. 365:810-816.
41. Spencer, M. 1969. Low-angle X-ray diffraction from concentrated sols of F-actin. Nature. 223:1361-1362.
42. Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
43. Stroobants, A., H. N. W. Lekkerkerker, and T. Odijk. 1986. Effect of electrostatic interaction on the liquid crystal phase transition in solutions of rodlike polyelectrolytes. Macromolecules. 19:2232-2238.
44. Suzuki, A., T. Maeda, and T. Ito. 1991. Formation of liquid crystalline phase of actin filament solutions and its dependence on filament length as studied by optical birefringence. Biophys. J. 59:25-30.
45. Suzuki, N., and K. Mihashi. 1991. Binding mode of cytochalasin B to F-actin is altered by lateral binding of regulatory proteins. J. Biochem. (Tokyo). 109:19-23.
46. Suzuki, A., M. Yamazaki, and T. Ito. 1989. Osmoelastic coupling in biological structures: formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stress. Biochemistry. 25: 6513-6518.
47. Tang, J. X., and P. A. Janmey. 1996. The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J. Biol. Chem. 271: 8556-8563.
48. Torbet, J., and M. J. Dickens. 1984. Orientation of skeletal muscle actin in strong magnetic fields. FEBS Lett. 173:403-406.
49. Yamashita, I., H. Suzuki, and K. Namba. 1998. Multiple-step method for making exceptionally well oriented liquid-crystalline sols of maromolecular assemblies. J. Mol. Biol. 278:609-615.
50. Yamashita, I., F. Vonderviszt, Y. Mimori, H. Suzuki, K. Oosawa, and K. Namba. 1995. Radial mass analysis of the flagellar filament of Salmonella: implications for the subunit folding. J. Mol. Biol. 253: 547-558.