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Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2020

Cooperatively enhanced reactivity and “stabilitaxis” of dissociating oligomeric proteins

Jaime Agudo-Canalejo
Ramin Golestanian

Résumé

Many functional units in biology, such as enzymes or molecular motors, are composed of several subunits that can reversibly assemble and disassemble. This includes oligomeric proteins composed of several smaller monomers, as well as protein complexes assembled from a few proteins. By studying the generic spatial transport properties of such proteins, we investigate here whether their ability to reversibly associate and dissociate may confer them a functional advantage with respect to non-dissociating proteins. In uniform environments with position-independent association-dissociation, we find that enhanced diffusion in the monomeric state coupled to reassociation into the functional oligomeric form leads to enhanced reactivity with localized targets. In non-uniform environments with position-dependent association-dissociation, caused e.g. by spatial gradients of an inhibiting chemical, we find that dissociating proteins generically tend to accumulate in regions where they are most stable, a process that we term stabilitaxis.
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Dates et versions

hal-03001328 , version 1 (13-11-2020)

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Jaime Agudo-Canalejo, Pierre Illien, Ramin Golestanian. Cooperatively enhanced reactivity and “stabilitaxis” of dissociating oligomeric proteins. Proceedings of the National Academy of Sciences of the United States of America, 2020, 117 (22), pp.11894-11900. ⟨10.1073/pnas.1919635117⟩. ⟨hal-03001328⟩
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