Cooperativity and Frustration in Protein-Mediated Parallel Actin Bundles

Abstract

We examine the mechanism of bundling of cytoskeletal actin filaments by two representative bundling proteins, fascin and espin. Small-angle X-ray studies show that increased binding from linkers drives a systematic \textit{overtwist} of actin filaments from their native state, which occurs in a linker-dependent fashion. Fascin bundles actin into a continuous spectrum of intermediate twist states, while espin only allows for untwisted actin filaments and fully-overtwisted bundles. Based on a coarse-grained, statistical model of protein binding, we show that the interplay between binding geometry and the intrinsic \textit{flexibility} of linkers mediates cooperative binding in the bundle. We attribute the respective continuous/discontinous bundling mechanisms of fascin/espin to differences in the stiffness of linker bonds themselves.

5 pages, 3 figures, figure file has been corrected in v2

References in corpus (2)

• Chirality and Equilibrium Biopolymer Bundles
• Packing defects and the width of biopolymer bundles

Cited by in corpus (8)

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• Crosslinked biopolymer bundles: crosslink reversibility leads to cooperative binding/unbinding phenomena