PMID: 2108725Feb 6, 1990Paper

19F NMR study of the myosin and tropomyosin binding sites on actin

Biochemistry
J A Barden, L Phillips

Abstract

Actin was labeled with pentafluorophenyl isothiocyanate at Lys-61. The label was sufficiently small not to affect the rate or extent of actin polymerization unlike the much larger fluorescein 5-isothiocyanate which completely inhibits actin polymerization [Burtnick, L. D. (1984) Biochim. Biophys. Acta 791, 57-62]. Furthermore, the label resonances in the 376.3-MHz 19F NMR spectrum were unaffected by actin polymerization. However, the binding of the relaxing protein tropomyosin resulted in the fluorinated Lys-61 resonances broadening out beyond detection due to a substantial increase in the effective correlation time of the label. Similarly, the binding of myosin subfragment 1 to F-actin resulted in the dramatic broadening of the labeled Lys-61 resonances. Thus, Lys-61 on actin appears to be closely associated with the binding sites for both tropomyosin and myosin, suggesting that both these proteins can compete for the same site on actin. The other region of actin known to be involved in myosin binding, Cys-10, was found to be more remote from the actin-actin interfaces than Lys-61. Labels on Cys-10 exhibited substantially greater mobility than fluorescein 5-isothiocyanate attached to Lys-61 which appeared to be held down on th...Continue Reading

Citations

Mar 14, 1995·Biochimica Et Biophysica Acta·C G dos Remedios, P D Moens
Sep 6, 1990·Nature·W KabschK C Holmes
Nov 1, 1992·NMR in Biomedicine·H R KalbitzerH Zimmermann
Mar 31, 1995·The Journal of Biological Chemistry·L BlanchoinD Pantaloni
Apr 1, 1992·Journal of Muscle Research and Cell Motility·M MikiC G Dos Remedios

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