Spectroscopic study of conformational changes in subdomain 1 of G- actin: Influence of divalent cations

Biophysical Journal

Volumn 73, Issue 4, 1997, Pages 2023-2032

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

^a UNIVERSITY OF PÉCS   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; G ACTIN; MAGNESIUM ION;

ANISOTROPY; ARTICLE; BINDING AFFINITY; BINDING SITE; CATION EXCHANGE; ELECTRON SPIN RESONANCE; FLUORESCENCE; LIGHT SCATTERING; MEASUREMENT; TEMPERATURE DEPENDENCE;

EID: 0030803626     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78232-8     Document Type: Article

References (67)

1. Alcala, J. R., E. Gratton, and F. G. Prendergast. 1987a. Resolvability of fluorescence lifetime distributions using phase fluorometry. Biophys. J. 51:587-596.
2. Alcala, J. R., E. Gratton, and F. G. Prendergast. 1987b. Fluorescence lifetime distributions in proteins. Biophys. J. 51:597-604.
3. Alcala, J. R., E. Gratton, and F. G. Prendergast. 1987c. Interpretation of fluorescence decays in proteins using continuous lifetime distributions. Biophys. J. 51:925-936.
4. Belford, G. G., R. L. Belford, and G. Weber. 1972. Dynamics of fluorescence polarization in macromolecules. Proc. Natl. Acad. Sci. USA. 69:1392-1393.
5. Bismuto, E., E. Gratton, and G. Irace. 1988. Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin. Biochemistry. 27:2132-2136.
6. Campbell, A. K. 1983. Intracellular Calcium. John Wiley, Chichester. 91.
7. Carlier, M. F. 1990. Actin polymerization and ATP hydrolysis. Adv. Biophys. 26:51-73.
8. Carlier, M. F., D. Pantaloni, and E. D. Korn. 1986. Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin. J. Biol. Chem. 261:10778-10784.
9. Demmer, D. R., D. R. James, R. P. Steer, and R. E. Verrall. 1987. Three exponential fluorescence decay of horse liver alcohol dehydrogenase revealed by iodide quenching. J. Photochem. Photobiol. 45:39-48.
10. Eftink, M. R., and C. A. Ghiron. 1976. Fluorescence quenching of indole and model micelle systems. J. Phys. Chem. 80:486-493.
11. 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.
12. Engh, R. A., L.-X. Chen, and G. R. Fleming. 1986. Conformational dynamics of tryptophan: a proposal for the origin of non-exponential fluorescence decay. Chem. Phys. Lett. 126:365-372.
13. Estes, J. E., L. A. Selden, and L. C. Gershman. 1987. Tight binding of divalent cations to monomeric actin. Binding kinetics support a simplified model. J. Biol. Chem. 262:4952-4957.
14. Estes, J. E., L. A. Selden, H. J. Kinosian, and L. C. Gershman. 1992. Tightly-bound divalent cation of actin. J. Muscle Res. Cell Motil. 13: 272-284.
15. Ferreira, S. T. 1989. Fluorescence studies of the conformational dynamics of parvalbumin in solution: lifetime and rotational motions of the single tryptophan residue. Biochemistry. 28:10066-10072.
16. Ferreira, S. T., and E. Gratton. 1990. Hydration and protein substates of proteins in reverse micelle. J. Mol. Liq. 43:253-272.
17. Ferreira, S. T., L. Stella, and E. Gratton. 1994. Conformational dynamics of bovine Cu, Zn superoxide dismutase revealed by time-resolved fluorescence spectroscopy of the single tyrosin residue. Biophys. J. 66: 1185-1196.
18. Feuer, G., F. Molnár, E. Pettkó, and F. B. Straub. 1948. Studies on the composition and polymerisation of actin. Hung. Acta Physiol. 1:150-163.
19. 2+-induced process at pH 8 and 20°C. Proc. Natl. Acad. Sci. USA. 80: 6513-6517.
20. 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.
21. 2+-induced conformational change requires ATP. Biochemistry. 24:4192-4196.
22. Gershman, L. C., L. A. Selden, H. J. Kinosian, and J. E. Estes. 1989. Preparation and polymerization properties of monomeric ADP-actin. Biochim. Biophys. Acta. 995:109-115.
23. Gershman, L. C., L. A. Selden, H. J. Kinosian, and J. E. Estes. 1991. High affinity divalent cation exchange on actin: association rate measurements support the simple competitive model. J. Biol. Chem. 266:76-82.
24. Goddette, D. W., E. C. Uberbacher, G. J. Bunick, and C. Frieden. 1986. Formation of actin dimers as studied by small angle neutron scattering. J. Biol. Chem. 261:2605-2609.
25. Goldman, S. A., G. V. Bruno, and J. H. Freed. 1972. Estimating slow-motional rotational correlation times for nitroxides by electron spin resonance. J. Phys. Chem. 76:1858-1860.
26. Gratton, E., N. Silva, and S. F. Ferreira. 1988. Fluorescence of tryptophan and protein dynamics. In Biological and Artificial Intelligence Systems. E. Clementi and S. Chin, editors. ESCOM Science Publishers, Leiden, The Netherlands. 49-56.
27. Houk, W. T., and K. Ue. 1974. The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62:66-74.
28. Hudson, E. N., and G. Weber. 1973. Synthesis and characterization of two fluorescent sulfhydryl reagents. Biochemistry. 12:4154-4161.
29. 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.
30. Israelachvili, J., J. Sjösten, L. E. G. Ericsson, M. Ehrström, A. Graslund, and A. Ehrenberg. 1974. Theoretical analysis of the molecular motion of spin labels in membranes. Biochim. Biophys. Acta. 339:164-172.
31. James, D. R., and W. R. Ware. 1985. A fallacy in the interpretation of fluorescence decay parameters. Chem. Phys. Lett. 120:455-459.
32. Jost, P., L. J. Libertini, V. C. Hebert, and O. H. Griffith. 1971. Lipid spin labels in lecithin multilayers. Study of motion along fatty acid chains. J. Mol. Biol. 59:77-98.
33. Kabsch, W., H. G. Mannherrz, D. Shuck, E. F. Pai, and K. C. Holmes. 1990. Atomic structure of actin: DNase I complex. Nature. 347:37-44.
34. Kasai, M., and F. Oosawa. 1968. The exchangeability of actin bound calcium with various divalent cations. Biochim. Biophys. Acta. 154: 520-528.
35. Kinosian, H. J., L. A. Selden, J. E. Estes, and L. C. Gershman. 1991. Thermodynamics of actin polymerization: influence of the tightly-bound cation. Biochim. Biophys. Acta. 1077:151-158.
36. Kinosita, K., S. Kawato, and A. Ikegami. 1977. A theory of fluorescence polarization decay in membranes. Biophys. J. 20:289-305.
37. Kitazawa, T., H. Shuman, and A. Somlyó. 1982. Calcium and magnesium binding to thin and thick filaments in skinned muscle fibers: electron probe analysis. J. Muscle Res. Cell Motil. 3:437-454.
38. Lakowicz, J. R. 1983a. Measurement of fluorescence lifetimes. In Principles of Fluorescence Spectroscopy. Plenum Press, New York and London. 52-95.
39. Lakowicz, J. R. 1983b. Quenching of fluorescence. In Principles of Fluorescence Spectroscopy. Plenum Press, New York and London. 258-304.
40. Lakowicz, J. R. 1991. Topics in fluorescence spectroscopy. Principles. Plenum Press, New York and London. 1-22.
41. Lipari, G., and A. Szabo. 1980. Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes. Biophys. J. 30:489-506.
42. Loscalzo, J., and G. H. Reed. 1976. Spectroscopic studies of actin-metal-nucleotide complexes. Biochemistry. 15:5407-5413.
43. Matkó, J., L. Trón, M. Balázs, J. Hevessy, B. Somogyi, and S. Damjanovich. 1980. Correlation between activity and dynamics of the protein matrix of phosphorylase b. Biochemistry. 19:5782-5786.
44. Mei, G., N. Rosato, N. Silva, Jr., R. Rusch, E. Gratton, I. Savini, and A. Finazzi-Agno. 1992. Denaturation of human Cu/Zn superoxide dismutase by guanidine hydrochloride: a dynamic fluorescence study. Biochemistry. 31:7224-7230.
45. 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.
46. Miki, M., and P. Wahl. 1985. Fluorescence energy transfer between points in G-actin: the nucleotide-binding site, the metal-binding site and Cys-374 residue. Biochim. Biophys. Acta. 828:188-195.
47. Montague, C., K. W. Rhee, and F. D. Carlson. 1983. Measurement of the translational diffusion constant of G-actin by photon correlation spectroscopy. J. Muscle Res. Cell Motil. 4:95-101.
48. 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.
49. Nowak, E., H. Strzelecka-Golaszewska, and R. Goody. 1988. Kinetics of nucleotide and metal ion interaction with G-actin. Biochemistry. 27: 1785-1792.
50. Orlova, A., and E. H. Egelman. 1992. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227:1043-1053.
51. Orlova, A., and E. H. Egelman. 1993. A conformational change in the actin subunit can change the flexibilty of the actin filament. J. Mol. Biol. 232:334-341.
52. Punyiczki, M., J. A. Norman, and A. Rosenberg. 1993. Interaction of acrylamide with proteins in the concentration range used for fluorescence quenching studies. Biophys. Chem. 47:9-19.
53. Rich, S. A., and J. E. Estes. 1976. Detection of conformational changes in actin by proteolytic digestion: evidence for a new monomeric species. J. Mol. Biol. 104:777-792.
54. Selden, L. A., J. E. Estes, and L. C. Gershman. 1989. High affinity divalent cation binding to actin. J. Biol. Chem. 264:9271-9277.
55. ++ bound at the high affinity site is a cofactor for actin ATPase activity. Biophys. J. 57:325a.
56. 1: a two-phase model for the quenching of protein fluorescence. Biochim. Biophys. Acta. 1209:61-68.
57. Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. J. Biol. Client. 246:4866-4871.
58. Stryer, L. 1968. Fluorescence spectroscopy of proteins. Science. 162: 526-533.
59. Strzelecka-Golaszewska, H. 1973. Relative affinities of divalent cations to the site of the tight calcium binding in G-actin. Biochim. Biophys. Acta. 310:60-69.
60. Strzelecka-Golaszewska, H., and W. Drabikowski. 1968. Studies on the exchange of G-actin-bound calcium with bivalent cations. Biochim. Biophys. Acta. 162:581-595.
61. 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.
62. Strzelecka-Golaszewska, H., E. Prochniewicz, and W. Drabikowski. 1978. Interaction of actin with divalent cations. 1. The effect of various cations on the physical state of actin. Eur. J. Biochem. 88:219-227.
63. Tao, T. 1969. Time-dependent fluorescence depolarization and Brownian rotational diffusion coefficients of macromolecules. Biopolymers. 8:609-632.
64. 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.
65. Tobacman, L. S., and E. D. Korn. 1983. The kinetics of actin nucleation and polymerization. J. Biol. Chem. 258:3207-3214.
66. Yanagida, T., M. Nakase, K. Nishiyama, and F. Oosawa. 1984. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature. 307:58-60.
67. Zimmerle, C. T., K. Patane, and C. Frieden. 1987. Divalent cation binding to the high- and low-affinity sites on G-actin. Biochemistry. 26: 6545-6552.