Parts | Days | Selection | Search | Updates | Downloads | Help
BP: Fachverband Biologische Physik
BP 33: Biological Machines \& Motor Proteins
BP 33.6: Talk
Friday, March 18, 2011, 12:00–12:15, ZEU 250
Actin filaments undergo local structural transitions at random sites — •Thomas Niedermayer1, Antoine Jegou2, Emmanuele Helfer2, Guillaume Romet-Lemonne2, Marie-France Carlier2, and Reinhard Lipowsky1 — 1Abteilung Theorie und Bio-Systeme, Max-Planck-Institut für Kolloid- und Grenzflächenforschung, 14424 Potsdam, Germany — 2Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France
After the polymerization of actin monomers into filaments, the actin-bound ATP is hydrolyzed into ADP, a process that is believed to decrease the filament stability. Recent experiments suggest the opposite behavior, however, namely that actin filaments become increasingly stable with time. Several mechanisms for this unexpected behavior have been proposed, ranging from structural transitions of the whole filament helix to pure artifacts arising, e.g., from the capping or surface attachment of the filament ends. We performed novel fluorescence microscopy experiments on single filaments to clarify this controversial issue. We find that filaments do indeed cease to depolymerize in an abrupt manner, and that this transition happens on relatively long time scales that exceed those of both ATP cleavage and phosphate release. We also developed a theory that allows us to distinguish the different possible transition mechanisms. A detailed comparison of theory and experiment implies that the sudden truncation of the shrinkage process does neither arise from artifacts nor from a collective transition of the whole filament. Instead, our results provide strong evidence for a local transition process occurring at random sites within the filament.