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We examine the mechanism of bundling of cytoskeletal actin filaments by tworepresentative bundling proteins, fascin and espin. Small-angle X-ray studiesshow that increased binding from linkers drives a systematic \textit{overtwist}of actin filaments from their native state, which occurs in a linker-dependentfashion. Fascin bundles actin into a continuous spectrum of intermediate twiststates, while espin only allows for untwisted actin filaments andfully-overtwisted bundles. Based on a coarse-grained, statistical model ofprotein binding, we show that the interplay between binding geometry and theintrinsic \textit{flexibility} of linkers mediates cooperative binding in thebundle. We attribute the respective continuous/discontinous bundling mechanismsof fascin/espin to differences in the stiffness of linker bonds themselves.

Cooperativity and Frustration in Protein-Mediated Parallel Actin Bundles