Fluorescence resonance energy transfer spectroscopy is a reliable “ruler” for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor

Journal of Structural Biology

Volumn 115, Issue 2, 1995, Pages 175-185

  Dos Remedios, Cristobal G ^a   Moens, Pierre D J ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE SPECTROSCOPY; MEASUREMENT; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW;

ACTINS; COMPUTER GRAPHICS; ENERGY TRANSFER; MOLECULAR PROBES; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SPECTROMETRY, FLUORESCENCE; SUPPORT, NON-U.S. GOV'T;

EID: 0028884014     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1006/jsbi.1995.1042     Document Type: Article

References (48)

1. Amir, D., and Haas, E, (1986) Determination of intramolecular distance distributions in a globular protein by nonradiative excitation energy transfer measurements, Biopolymers 25, 235-240
2. Aspenstrom, P., Lindberg, U., and Karlsson, R. (1992) Site-specific amino-terminal mutants of yeast-expressed fi-actin: Characterization of the interaction with myosin and tropomyosin, FEBS Lett. 303, 59-63
3. 2+ exchange as detected by proton NMR spectroscopy, Eur. J. Biochem. 146, 5-8
4. Barden, J. A., Miki, M., and dos Remedios, C. G. (1986) Selective labeling of Cys-10 on actin, Biochem. Int. 12, 95-101
5. Botts, J., Takashi, R., Torgerson, P., Hozumi, T., Muhlrad, A., Mornet, D., and Morales, M. F, (1984) On the mechanism of energy transduction in myosin sub fragment 1, Proc. Natl. Acad. Sci. USA 81, 2060-2064
6. Burtnick, L. D, (1984) Modification of actin with fluorescein isothiocyanate, Biochim. Biophys. Acta 791, 57-62
7. Dale, R. E., Eisinger, J., and Blumberg, W. E. (1979) The orientational freedom of molecular probes: The orientation factor in intramolecular energy transfer, Biophys. J. 26, 161-194
8. dos Remedios, C. G. (1981) Lanthanide ion probes of calciumbinding sites on cellular membranes, Cell Calcium 2, 29-51
9. dos Remedios, C. G., Miki, M., and Barden, J. A. (1987) Fluorescence resonance energy transfer measurements of distances in actin and myosin: A critical evaluation, J. Muscle Res. Cell Motil 8, 97-117
10. dos Remedios, C. G., Kiessling, P. C., and Hambly, B. D. (1994) DNase I binding induces a conformational change in the actin monomer, in Chance, B. et al. (Eds.), Synchrotron Radiation in the Biosciences, pp. 418-425, Oxford Univ. Press, Oxford
11. dos Remedios, C. G., and Moens, P. D. J. (1995) Actin and the actomyosin interface: a review, Biochim. Biophys. Acta 1228, 99-124
12. Drewes, G., and Faulstich, H. (1991). A reversible conformational transition in muscle actin is caused by nucleotide exchange and uncovers cysteine in position 10, J. Biol. Chem. 266, 5508-5513
13. Elofsson, A., Rigler, R., Nilsson, L., Roslund, J., Krause, G., and Holmgren, A. (1991) Motion of aromatic side chains, picosecond fluorescence, and internal energy transfer in Escherichia coli thioredoxin studied by site-directed mutagenesis, time resolved fluorescence spectroscopy, and molecular dynamics simulations, Biochemistry 30, 9648-9656
14. Fernandez, S. M., and Berlin, R. D. (1976) Cell surface distribution of lectin receptors determined by resonance energy transfer, Nature 264, 411-415
15. Forster, T. (1948) Zwischenmolekulare Energiwanderung und Fluoreszence [Intermolecular energy migration and fluorescence], Ann. Phys. 2, 55-75
16. Forster, T. (1965) Delocalized excitation and excitation transfer, in Sinanoglu, O. (Ed.), Modern Quantum Chemistry. Istanbul Lectures. Part III: Action of Light, and Organic Crystals, pp. 93-137, Academic Press, New York
17. Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., and Yanagida, T, (1995) Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution, Nature 374, 555-559
18. Gryczynski, Z., Tennenholz, T., and Bucci, E. (1992) Rates of energy transfer between tryptophans and hemes in hemoglobin, assuming that the heme is a planar oscIIIator, Biophys. J. 63, 648-653
19. Hanson, J. (1967) Axial period of actin filaments, Nature 213, 353-356
20. Hanson, J., Lednev, V., O’Brien, E. J., and Bennett, P. M. (1972) Structure of actin-containing filaments in vertebrate skeletal muscle, Cold Spring Harbor Symp. Quant. Biol. 37, 311-318
21. Haughland, R. P. (1992) Molecular Probes Handbook of Fluorescent Probes and Research Chemicals, Molecular Probes, Inc., Eugene, Oregon
22. Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., and Holmes, K. C. (1990) Atomic structure of the actin-DNase I complex, Nature 347, 37-44
23. Kasprzak, A. A., Takashi, R., and Morales, M. F, (1988). Orientation of the actin monomer in the F-actin filament: Radial coordinate of glutamine-41 and effect of myosin subfragment-1 binding on the monomer orientation, Biochemistry 27, 4512-4522
24. Kasumi, A., Tsuji, A., Murata, M., Sako, Z., Yoshizawa, A. C., Dagiwada, S., Hayakawa, T., and Ohnishi, S. (1991) Development of a streak-camera-based time-resolved microscope fluo-rimeter and its application to studies of membrane fusion in single cells, Biochemistry 30, 6517-6527
25. Lakowicz, J. R. (1983) Principles of Fluorescence Spectroscopy, Plenum, New York
26. Lorenz, M., Popp, D., and Holmes, K. C. (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
27. McLaughlin, P. J., Gooch, J. T., Mannherz, H. G., and Weeds, A. G. (1993) Structure of gelsolin segment-1-actin complex and the mechanism of filament severing, Nature 364, 685-692
28. Miki, M., and Ohnuma, H. (1974) Interaction of actin with e-ADP, FEBS Lett. 46, 17-19
29. Miki, M., Kouyama, T., and Mihashi, K. (1976) Fluorescence study of e-ADP bound to rabbit F-actin: Structural change in the adenine subsite of F-actin under the influence of heavy mero-myosin, FEBS Lett. 66, 98-101
30. Miki, M., and Mihashi, K. (1978) Fluorescence energy transfer between e-ADP at nucleotide binding site and 7V-(4-dimethyl-amino-3, 5-dinitrophenyl)maleimide at Cys-373 of G-actin, Biochim. Biophys. Acta 533, 163-172
31. Miki, M., and Wahl, P. (1985) Fluorescence energy transfer between points in G-actin: The nucleotide binding site, the metal binding site and Cys-373 residue, Biochim. Biophys. Acta 828, 188-195
32. Miki, M., Hambly, B. D., and dos Remedios, C. G. (1986) Fluorescence energy transfer between nucleotide binding sites in an F-actin filament, Biochim. Biophys. Acta 871, 137-141
33. Miki, M., Barden, J. A., dos Remedios, C. G., PhIIIips, L., and Hambly, B. D. (1987) Interaction of phalloidin with chemically modified actin, Eur. J. Biochem. 165, 125-130
34. Miki, M., and dos Remedios, C. G. (1990) A determination of the radial coordinate of Tyr-69 in F-actin using fluorescence energy transfer, Biochem. Int. 22, 125-132
35. Miki, M., O’Donoghue, S. I., and dos Remedios, C. G. (1992) Structure of actin observed by fluorescence resonance energy transfer spectroscopy, J. Muscle Res. Cell Motil. 13, 132-145
36. Moens, P. D. J., Yee, D., and dos Remedios, C. G. (1994) Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: Effect of phalloidin on polymer assembly, Biochemistry 33, 13102-13108
37. O’Donoghue, S. I., Hambly, B. D., and dos Remedios, C. G. (1992) Models of actin monomer and filament from fluorescence resonance-energy transfer, Eur. J. Biochem. 205, 591-601
38. Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C., and MIIIigan, R. A. (1993) Structure of the actin-myosin complex and its implications for muscle contraction, Science 261, 58-65
39. Saito, K., Aoki, T., and Yanagida, T. (1994) Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap, Biophys. J. 66, 769-777
40. Sasaki, K., Sakabe, K., Sakabe, N., Kondo, H., and Shimomura, M. (1992) Crystal structure of smooth muscle actin DNase I complex at 2 A resolution. Proc. 4th Int. Conf. Biophys. Synchrotron Radiation, 29, Tsukuba, Japan
41. Schutt, C. E., Myslik, J. C., Rozycki, M. D., Goonesekere, N., and Lindberg, U. (1993) The structure of crystalline profilin-(3-actin, Nature 365, 810-816
42. Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler, Annu. Rev. Biochem. 47, 819-846
43. Stryer, L., and Haugland, R. P. (1967) Energy transfer: A spectroscopic ruler, Proc. Natl. Acad. Sci. USA 58, 716-726
44. Takashi, R. (1988) A novel actin label: A fluorescent probe at glutamine 41 and its consequences, Biochemistry 27, 938-943
45. Taylor, D. L., Reidler, J., Spudich, J. A., and Stryer, L. (1981) Detection of actin assembly by fluorescence energy transfer, J. Cell Biol. 89, 362-367
46. Turina, P., and Capaldi, R. A. (1994) ATP hydrolysis-driven structural changes in the (3-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues, J. Biol. Chem. 269, 13465-13471
47. Vanderkerckhove, J., and Weber, K. (1979) The amino acid sequence of actin from chicken skeletal and chicken gizzard smooth muscle, FEBS Lett. 102, 219-222
48. Van Der Meer, B. W., Coker, G. III, and Chen, S.-Y. (1994) Resonance Energy Transfer Theory and Data, VCH, New York