The influence of divalent cations on the dynamic properties of actin filaments: A spectroscopic study

Biophysical Journal

Volumn 75, Issue 6, 1998, Pages 3015-3022

  Hild, G ^a   Nyitrai, M ^a   Belagyi J ^a   Somogyi, B ^a,b  

^a UNIVERSITY OF PÉCS   (Hungary)

^b NONE   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM ION; CATION; CYSTEINE PROTEINASE; MAGNESIUM ION;

ACTIN FILAMENT; ANIMAL TISSUE; ANISOTROPY; ARTICLE; ELECTRON SPIN RESONANCE; FLUOROMETRY; MUSCLE CONTRACTION; NONHUMAN; PROTEIN CONFORMATION; RABBIT; SKELETAL MUSCLE; TEMPERATURE DEPENDENCE;

ANIMALIA; ARRHENIUS; ORYCTOLAGUS CUNICULUS;

EID: 0031770440     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77742-2     Document Type: Article

References (41)

1. Belford, G. G., R. L. Belford, and G. Weber. 1972. Dynamics of fluorescence polarization in macromolecules. Proc. Natl. Acad. Sci. USA. 69(6):1392-1393.
2. Elzinga, M., J. H. Collins, W. M. Kuehl, and R. S. Adelstein. 1973. Complete amino-acid sequence of actin of rabbit skeletal muscle. Proc. Natl. Acad. Sci. USA. 70:2687-2691.
3. Fajer, P., and D. Marsh. 1982. Microwave and modulation field inhomogenities and effect of cavity Q in saturation transfer EPR spectra: dependence of sample size. J. Magn. Reson. 49:212-224.
4. Feuer, G., F. Molnár, E. Pettkó, and F. B. Straub. 1948. Studies on the composition and polymerisation of actin. Hung. Acta Physiol. I:150-163.
5. Frieden, C., D. Lieberman, and H. R. Gilbert. 1980. Fluorescence probe for conformational changes in skeletal muscle G-actin. J. Biol. Chem. 255: 8991-8993.
6. Fujime, S., and S. Ishiwata. 1971. Dynamic study of F-actin by quasielastic scattering of laser light. J. Mol. Biol. 62:251-265.
7. Geeves, M. A. 1991. The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem. J. 274:1-14
8. Hegyi, Gy., L. Szilágyi, and J. Belágyi. 1988. Influence of the bound nucleotide on the molecular dynamics of actin. Eur. J. Biochem. 175: 271-274.
9. Heintz, D., H. Kany, and H. R. Kalbitzer. 1996. Mobility of the N-terminal segment of rabbit skeletal muscle F-actin detected by 1H and 19F nuclear magnetic resonance spectroscopy. Biochemistry. 35: 12686-12693.
10. Horváth, L. I., and D. Marsh. 1983. Analysis of multicomponent saturation transfer ESR spectra using integral method: application to membrane systems. J. Magn. Reson. 54:363-373.
11. Houk, W. T., and K. Ue. 1974. The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62:66-74.
12. Hudson, E. N., and G. Weber. 1973. Synthesis and characterization of two fluorescent sulfhydryl reagents. Biochemistry. 12:4154-61.
13. Ikkai, T., P. Wahl, and J. C. Auchet. 1979. Anisotropy decay of labeled actin. Evidence of the flexibility of the peptide chain in F-actin molecules. Eur. J. Biochem. 93:397-408.
14. 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. J. Biol. Chem. 270(19):11437-11444.
15. Kawamura, M., and K. Maruyama. 1970. Electron microscopic particle length of F-actin polymerized in vitro. J. Biochem. (Tokyo). 67: 437-457.
16. Kawasaki, Y., K. Mihashi, H. Tanaka, and H. Ohnuma. 1976. Fluorescence study of N-(3-pyrene)maleimide conjugated to rabbit skeletal F-actin and plasmodium actin polymers. Biochim. Biophys. Acta. 446:166-178.
17. Lakowicz, J. R. 1983. Measurements of fluorescence lifetimes. In Principles of Fluorescence Spectroscopy. Plenum Press, New York and London. 52-95.
18. -3 s time range studied by transient absorption anisotropy: detection of torsional motion. J. Biochem. (Tokyo) 93:1705-1707.
19. Mihashi, K., and P. Wahl. 1975. Nanosecond pulsefluorometry in polarized light of G-actin-epsilon-ATP and F-actin-epsilon-ADP. FEBS Lett. 52: 8-12.
20. Miki M., C. G. dos Remedios, and J. A. Barden. 1987. Spatial relationship between the nucleotide-binding site, Lys-61 and Cys-374 in actin and a conformational change induced by myosin subfragment-1 binding. Eur. J. Biochem. 168:339-345.
21. 2+ on the flexibility of F-actin. Biophys. Chem. 16:165-172.
22. Miki, M., P. Wahl, and J.-C. Auchet. 1982b. Fluorescence anisotropy of labeled F-actin: Influence of divalent cations on the interaction between F-actin and myosin heads. Biochemistry. 21:3661-3665.
23. Mossakowska, M., J. Belágyi, and H. Strzelecka-Golaszewska. 1988. An EPR study of the rotational dynamics of actins from striated and smooth muscle and their complexes with heavy meromyosin. Eur. J. Biochem. 175:557-564.
24. Nyitrai, M., G. Hild, J. Belágyi, and B. Somogyi. 1997. Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations. Biophys. J. 73:2023-2032.
25. 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.
26. Orlova A., and E. H. Egelman. 1995. Structural dynamics of F-actin: I. Changes in the C terminus. J. Mol. Biol. 245(5):582-97.
27. Prochniewicz, E., and T. Yanagida. 1990. Inhibition of sliding movement of F-actin by cross-linking emphasizes the role of F-actin structure in the mechanism of motility. J. Mol. Biol. 216:761-772.
28. Rayment, I., H. 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.
29. Scharf, R. E., and J. Newman. 1995. Mg-and Ca-actin filaments appear virtually identical in steady-state as determined by dynamic light scattering. Biochim. Biophys. Acta. 1253:129-132.
30. Schutt, C. E., M. D., Rozycki, J. K., Chick, and U. Lindberg. 1995. Structural studies on the ribbon-to-helix transition in profilin: actin crystals. Biophys. J. 68:12s-18s.
31. Somogyi, B., J., Matkó, S., Papp, J., Hevessy, G. R., Welch, and S., Damjanovich. 1984. Förster-type energy transfer as a probe for changes in local fluctuations of protein matrix. Biochemistry. 23:3403-3411.
32. 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.
33. Squire, T. C., and D. D. Thomas. 1986. Methodology for increased precision in saturation transfer electron paramagnetic resonance studies of rotational dynamics. Biophys. J. 49:921-935.
34. Steinmetz, M. O., K. N. Goldie, and U. Aebi. 1997. A correlative analysis of actin filament assembly, structure and dynamics. J. Cell Biol 138: 559-574.
35. Stryer, L. 1968. Fluorescence spectroscopy of proteins. Science. 162: 526-533.
36. Strzelecka-Golaszewska, H., J. Moraczewska, S. Y. Khaitlina, and M. Mossakowska. 1993. Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur. J. Biochem. 211:731-742.
37. Tawada, K., P. Wahl, and J.-C. Auchet. 1978. Study of actin and its interaction with heavy meromyosin and regulatory proteins by the pulse fluorimetry in polarized light of a fluorescent probe attached to an actin cysteine. Eur. J. Biochem. 88:411-419.
38. Thomas, D. D., J. C. Seidel, and J. Gergely. 1979. Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range. J. Mol. Biol. 132:257-273.
39. Trayer, I. P., H. R., Trayer, and B. A Levine. 1987. Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. Eur. J. Biochem. 164:259-266.
40. Wahl, P., K. Mihashi, and J. C. Auchet. 1975. Nanosecond pulse fluorometry in polarized light of dansyl-L-cysteine linked to a unique SH group of F-actin; the influence of regulatory proteins and myosin moiety. FEBS Lett. 60:164-167.
41. Yasuda, R., H. Miyata, and K. Kinosita Jr. 1996. Direct measurement of torsional rigidity of single actin filaments. J. Mol. Biol. 263:227-236.