A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using μg quantities of protein

Journal of Muscle Research and Cell Motility

Volumn 17, Issue 6, 1996, Pages 669-676

  Kurzawa, Susanne E ^a   Geeves, Michael A ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN; PHALLOIDIN;

ANIMAL TISSUE; CONFERENCE PAPER; CONTROLLED STUDY; DISSOCIATION CONSTANT; FLUORESCENCE; IN VITRO STUDY; MUSCLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RABBIT; SPECTROPHOTOMETRY; TECHNIQUE;

ACTINS; ACTOMYOSIN; ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING, COMPETITIVE; DOSE-RESPONSE RELATIONSHIP, DRUG; FLUOROMETRY; MYOSIN SUBFRAGMENTS; MYOSINS; PHALLOIDINE; PYRENES; RABBITS;

EID: 0030472486     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00154061     Document Type: Conference Paper

References (26)

1. AGUIRRE, R., GONSOULIN, F. & CHEUNG, H. C. (1986) Interaction of fluorescently labeled myosin subfragment 1 with nucleotides and actin. Biochemistry 25, 6827-35.
2. COATES, J. H., CRIDDLE, A. H. & GEEVES, M. A. (1985) Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment 1 from rabbit skeletal muscle. Biochem. J. 232, 351-6.
3. CONIBEAR, P. B. (1993) Solution Studies on the interactions between the two heads of heavy meromyosin and on the effect of ADP on the interaction of myosin subfragment 1 with actin. PhD thesis, Bristol.
4. 2 terminus. J. Biol. Chem. 268, 2410-15.
5. CRIDDLE, A. H., GEEVES, M. A. & JEFFRIES, T. (1985) The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem. J. 232, 343-9.
6. DANCKER, P., LOW, I., HASSELBACH, W. & WIELAND, T. (1975) Interaction of actin with phalloidin: polymerization and stabilization of F-actin. Biochim. Biophys. Acta 400, 407-14.
7. GEEVES, M. A. & JEFFRIES, T. E. (1988) The effect of nucleotide upon a specific isomerization of actomyosin subfragment 1. Biochem. J. 256, 41-6.
8. HIGHSMITH, S., MENDELSON, R. A. & MORALES, M. F. (1976) Affinity of myosin S-1 for F-actin, measured by time-resolved fluorescence anisotropy. Proc. Natl Acad. Sci. USA 73, 133-7.
9. KONRAD, M. & GOODY, R. S. (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, 547-55.
10. KOUYAMA, T. & MIHASHI, K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Eur. J. Biochem. 114, 33-8.
11. KRON, S. J. & SPUDICH, J. A. (1986) Fluorescent actin filaments move on myosin fixed to a glass surface. Biochemistry 83, 6272-6.
12. LEHRER, S. S. & KERWAR, G. (1972) Intrinsic fluorescence of actin. Biochemistry 11, 1211-17.
13. MANSTEIN, D. J. & HUNT, D. M. (1995) Overexpression of myosin motor domains in Dictyostelium: screening of transformants and purification of the affinity tagged protein. J. Muscle Res. Cell Motil. 16, 325-32.
14. MANSTEIN, D. J., RUPPEL, K. M. & SPUDICH, J. A. (1989) Expression and characterization of a functional myosin head fragment in Dictyostelium discoideum. Science 246, 656-8.
15. MARGOSSIAN, S. S. & LOWEY, S. (1978) Interaction of myosin subfragments with F-actin. Biochemistry 17, 5431-9.
16. MARSTON, S. B. (1982) The rates of formation and dissociation of actin-myosin complexes. Biochem. J. 203, 453-60.
17. MARSTON, S. & WEBER, A. (1975) The dissociation constant of the actin-heavy meromyosin subfragment-1 complex. Biochemistry 14, 3868-73.
18. MILLER, C. J. & REISLER, E. (1995) Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin. Biochemistry 34, 2694-700.
19. PATO, M. D., SELLERS, J. R., PRESTON, Y. A., HARVEY, E. V. & ADELSTEIN, R. S. (1996) Baculovirus expression of chicken nonmuscle heavy meromyosin II-B. J. Biol. Chem. 271, 2689-95.
20. SPARROW, J., DRUMMOND, D., PECKHAM, M., HENNESSEY, E. & WHITE, D. (1991) Protein engineering and the study of muscle contraction in Drosophila flight muscle. J. Cell Sci. 14, 73-8.
21. SUTOH, K., ANDO, M., SUTOH, K. & TOYOSHIMA, Y. Y. (1991) Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N terminus. Proc. Natl Acad. Sci. USA 88, 7711-14.
22. SWEENEY, H. L., STRACESKI, A. J., LEINWAND, L. A., TIKUNOV, B. A. & FAUST, L. (1994) Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction. J. Biol. Chem. 269, 1603-5.
23. TRYBUS, K. M. (1994) Regulation of expressed truncated smooth muscle myosins. J. Biol. Chem. 269, 20819-22.
24. WEEDS, A. G. & TAYLOR, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 257, 54-7.
25. WEST, J. J., NAGY, B. & GERGELEY, J. (1967) The effect of EDTA on spectral properties of ATP-, ADP-, and ITP-G-actin. Biochem. Biophys. Ref. Commun. 29, 611-29.
26. WHITE, H. D. & TAYLOR, E. W. (1976) Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15, 5818-26.