Monitoring the myosin ATPase reaction using a sensitive fluorescent probe: Pyrene-labeled ATP

Biophysical Journal

Volumn 72, Issue 2 I, 1997, Pages 843-849

  Hiratsuka, Toshiaki ^a  

^a ASAHIKAWA MEDICAL COLLEGE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MYOSIN;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME BINDING; FLUORESCENCE; MUSCLE CONTRACTION; NONHUMAN; PROTEIN PROTEIN INTERACTION; RABBIT; SPECTROSCOPY; STRUCTURE ANALYSIS;

EID: 0031013418     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78718-6     Document Type: Article

References (37)

1. Anson, M., D. R. Drummond, M. A. Geeves, E. S. Hennessey, M. D. Ritchie, and J. C. Sparrow. 1995. Actomyosin kinetics and in vitro motility of wild-type Drosophila actin and the effects of two mutations in the Act88F gene. Biophys. J. 68:1991-2003.
2. Barrantes, F. J., B. Sakmann, R. Bonner, H. Eibl, and T. M. Jovin. 1975. 1-Pyrene-butyrylcholine: a fluorescent probe for the cholinergic system. Proc. Natl. Acad. Sci. USA. 72:3097-3101.
3. Chance, B. 1957. A simple relationship for a calculation of the "on" velocity constant in enzyme reactions. Arch. Biochem. Biophys. 71: 130-136.
4. Conibear, P. B., D. S. Jeffreys, C. K. Seehra, R. J. Eaton, and C. R. Bagshaw. 1996. Kinetic and spectroscopic characterization of fluorescent ribose-modified ATP analogs upon interaction with skeletal muscle myosin subfragment 1. Biochemistry. 35:2299-2308.
5. 2 cross-linking. Biochemistry. 29:3309-3319.
6. Fiske, C. H., and Y. Subbarow. 1925. Phosphorus assay. J. Biol. Chem. 66:375-400.
7. Franks-Skiba, K., and R. Cooke. 1995. The conformation of the active site of myosin probed using mant-nucleotides. Biophys. J. 68:142s-149s.
8. Funatsu, T., Y. Harada, M. Tokunaga, K. Saito, and T. Yanagida. 1995. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature. 374:555-559.
9. Goodno, C. C., and E. W. Taylor. 1982. Inhibition of actomyosin ATPase by vanadate. Proc. Natl. Acad. Sci. USA. 79:21-25.
10. Haugland, R. P. 1992. In Handbook of Fluorescent Probes and Research Chemicals, Molecular Probes, Eugene, OR. 5-22.
11. Hiratsuka, T. 1976. Fluorescence properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl)adenosine 5′-triphosphate and its use in the study of binding to heavy meromyosin ATPase. Biochim. Biophys. Acta. 453: 293-297.
12. Hiratsuka, T. 1983. New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta. 742:496-508.
13. Hiratsuka, T. 1984. Affinity labeling of the myosin ATPase with ribose-modified fluorescent nucleotides and vanadate. J. Biochem. (Tokyo). 96:147-154.
14. 2-terminal peptide segment of myosin ATPase associated with ATP hydrolysis. J. Biol. Chem. 265:18786-18790.
15. Hiratsuka, T., and K. Uchida. 1973. Preparation and properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl)adenosine 5′-triphosphate, an analog of adenosine triphosphate. Biochim. Biophys. Acta. 320:635-647.
16. Inaba, K., M. Okuno, and H. Mohri. 1989. Anthraniloyl ATP, a fluorescent analog of ATP, as a substrate for dynein ATPase and flagellar motility. Arch. Biochem. Biophys. 274:209-215.
17. Kierzek, R., Y. Li, D. H. Turner, and P. C. Bevilacqua. 1993. 5′-Amino pyrene provides a sensitive, nonperturbing fluorescent probe of RNA secondary and tertiary structure formation. J. Am. Chem. Soc. 115: 4985-4992.
18. Knopp, J. A., and G. Weber. 1969. Fluorescence polarization of pyrenebutyric-bovine serum albumin and pyrenebutyric-human macroglobulin conjugates. J. Biol. Chem. 244:6309-6315.
19. Konrad, M., and R. S. Goody. 1982. Kinetic and thermodynamic properties of the ternary complex between F-actin, myosin subfragment 1 and adenosine 5′-[β,γ-imido]triphosphate. Eur. J. Biochem. 128:547-555.
20. Kouyama, T., and K. Mihashi. 1981. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin: local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114:33-38.
21. Lockhart, A., and R. A. Cross. 1996. Kinetics and motility of the Eg5 microtubule motor. Biochemistry. 35:2365-2373.
22. Ma, Y.-Z., and E. W. Taylor. 1995. Kinetic mechanism of kinesin motor domain. Biochemistry. 34:13233-13241.
23. Morrison, L. E., T. C. Halder, and L. M. Stols. 1989. Solution-phase detection of polynucleotides using interacting fluorescent labels and competitive hybridization. Anal. Biochem. 183:231-244.
24. Perry, S. V. 1955. Myosin adenosinetriphosphatase. Methods Enzymol. 2:582-588.
25. Ritchie, M. D., M. A. Geeves, S. K. A. Woodward, and D. J. Manstein. 1993. Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum. Proc. Natl. Acad. Sci. USA. 90:8619-8623.
26. Rosenfeld, S. S., J. Xing, B. Rener, J. Lebowitz, S. Kar, and H. C. Cheung. 1994. Structural and kinetic studies of the 10 S ↔ 6 S transition in smooth muscle myosin. J. Biol. Chem. 269:30187-30194.
27. Sadhu, A., and E. W. Taylor. 1992. A kinetic study of the kinesin ATPase. J. Biol. Chem. 267:11352-11359.
28. Shimizu, T., E. Sablin, R. D. Vale, R. Fletterick, E. Pechatnikova, and E. W. Taylor. 1995. Expression, purification, ATPase properties, and microtubule-binding properties of the ncd motor domain. Biochemistry. 34:13259-13266.
29. Somerharju, P. J., J. A. Virtanen, K. K. Eklund, P. Vainio, and P. K. J. Kinnunen. 1985. 1-Palmitoyl-2-pyrenedecanoyl glycerophospholipids as membrane probes: evidence for regular distribution in liquid-crystalline phosphatidylcholine bilayers. Biochemistry. 24:2773-2781.
30. Sowerby, A. J., C. K. Seehra, M. Lee, and C. R. Bagshaw. 1993. Turnover of fluorescent nucleoside triphosphates by isolated immobilized myosin filaments: transient kinetics on the zeptomole scale. J. Mol. Biol. 234: 114-123.
31. Wagner, P. D., and A. G. Weeds. 1977. Studies on the role of myosin light chains. J. Mol. Biol. 109:455-473.
32. Weeds, A. G., and R. S. Taylor. 1975. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature. 257:54-56.
33. Wells, C., and C. R. Bagshaw. 1984. The characterization of vanadate-trapped nucleotide complexes with spin-labelled myosins. J. Muscle Res. Cell Motil. 5:97-112.
34. Weltman, J. K., R. P. Szaro, A. R. Frackelton, Jr., R. M. Dowben, J. R. Bunting, and R. E. Cathou. 1973. N-(3-Pyrene)maleimide: a long life-time fluorescent sulfhydryl reagent. J. Biol. Chem. 248:3173-3177.
35. Woodward, S. K. A., J. F. Eccleston, and M. A. Geeves. 1991. Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: characterization of two acto · S1 · ADP complexes. Biochemistry. 30:422-430.
36. Woodward, S. K. A., M. A. Geeves, and D. J. Manstein. 1995. Kinetic characterization of the catalytic domain of Dictyostelium discoideum. Biochemistry. 34:16056-16064.
37. Yount, R. G. 1975. ATP analogs. Adv. Enzymol. 43:1-56.