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Interaction of actin with phalloidin:: Polymerization and stabilization of F-actin

MPG-Autoren
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Dancker,  Peter
Max Planck Institute for Medical Research, Max Planck Society;

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Löw,  Irmentraut
Max Planck Institute for Medical Research, Max Planck Society;

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Hasselbach,  Wilhelm
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wieland,  Theodor
Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Dancker, P., Löw, I., Hasselbach, W., & Wieland, T. (1975). Interaction of actin with phalloidin: Polymerization and stabilization of F-actin. Biochimica et Biophysica Acta: BBA, 400(2), 407-414. doi:10.1016/0005-2795(75)90196-8.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002D-FC49-E
Zusammenfassung
The cyclic peptide phalloidin, one of the toxic components of Amanita phalloides prevented the drop of viscosity of F-actin solutions after the addition of 0.6 M KI and inhibited the ATP splitting of F-actin during sonic vibration. The data concerning ATP splitting are consistent with the assumption (a) that only 1 out of every 3 actin units of the filaments needs to be combined with phalloidin in order to suppress the contribution of these 3 actins to the ATPase activity of the filament and (b) that all actin units of the filaments can combine with phalloidin with a very high affinity. Phalloidin did not only stabilize the actin-actin bonds in the F-actin structure but it also increased the rate of polymerization of G-actin to F-actin. The ability of F-actin to activate myosin ATPase was not affected by phalloidin. The tropomyosin-troponin complex did not prevent the stabilizing effect of phalloidin on the F-actin structure.