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Probing time-dependent mechanical behaviors of catch bonds based on two-state models.

ABSTRACT: With lifetime counter-intuitively being prolonged under forces, catch bonds can play critical roles in various sub-cellular processes. By adopting different "catching" strategies within the framework of two-state models, we construct two types of catch bonds that have a similar force-lifetime profile upon a constant force-clamp load. However, when a single catch bond of either type is subjected to varied forces, we find that they can behave very differently in both force history dependence and bond strength. We further find that a cluster of catch bonds of either type generally becomes unstable when subjected to a periodically oscillating force, which is consistent with experimental results. These results provide important insights into versatile time-dependent mechanical behaviors of catch bonds. We suggest that it is necessary to further differentiate those bonds that are all phenomenologically referred to as "Catch bonds".

SUBMITTER: Chen X

PROVIDER: S-EPMC4297987 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature

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Probing time-dependent mechanical behaviors of catch bonds based on two-state models.

Chen Xiaofeng X Mao Zhixiu Z Chen Bin B

Scientific reports 20150119

With lifetime counter-intuitively being prolonged under forces, catch bonds can play critical roles in various sub-cellular processes. By adopting different "catching" strategies within the framework of two-state models, we construct two types of catch bonds that have a similar force-lifetime profile upon a constant force-clamp load. However, when a single catch bond of either type is subjected to varied forces, we find that they can behave very differently in both force history dependence and b ...[more]

PMID: 25598078

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Project description:Cellular structures are continually subjected to forces, which may serve as mechanical signals for cells through their effects on biomolecule interaction kinetics. Typically, molecular complexes interact via "slip bonds," so applied forces accelerate off rates by reducing transition energy barriers. However, biomolecules with multiple dissociation pathways may have considerably more complicated force dependencies. This is the case for DNA-binding proteins that undergo "facilitated dissociation," in which competitor biomolecules from solution enhance molecular dissociation in a concentration-dependent manner. Using simulations and theory, we develop a generic model that shows that proteins undergoing facilitated dissociation can form an alternative type of molecular bond, known as a "catch bond," for which applied forces suppress protein dissociation. This occurs because the binding by protein competitors responsible for the facilitated dissociation pathway can be inhibited by applied forces. Within the model, we explore how the force dependence of dissociation is regulated by intrinsic factors, including molecular sensitivity to force and binding geometry and the extrinsic factor of competitor protein concentration. We find that catch bonds generically emerge when the force dependence of the facilitated unbinding pathway is stronger than that of the spontaneous unbinding pathway. The sharpness of the transition between slip- and catch-bond kinetics depends on the degree to which the protein bends its DNA substrate. This force-dependent kinetics is broadly regulated by the concentration of competitor biomolecules in solution. Thus, the observed catch bond is mechanistically distinct from other known physiological catch bonds because it requires an extrinsic factor-competitor proteins-rather than a specific intrinsic molecular structure. We hypothesize that this mechanism for regulating force-dependent protein dissociation may be used by cells to modulate protein exchange, regulate transcription, and facilitate diffusive search processes.

Dataset Information

Probing time-dependent mechanical behaviors of catch bonds based on two-state models.

Publications

Probing time-dependent mechanical behaviors of catch bonds based on two-state models.

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