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  Cooperatively enhanced reactivity and “stabilitaxis” of dissociating oligomeric proteins

Agudo-Canalejo, J., Illien, P., & Golestanian, R. (2020). Cooperatively enhanced reactivity and “stabilitaxis” of dissociating oligomeric proteins. Proceedings of the National Academy of Sciences, 117(22), 11894-11900. doi:10.1073/pnas.1919635117.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-96E4-F Version Permalink: http://hdl.handle.net/21.11116/0000-0006-96E5-E
Genre: Journal Article

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 Creators:
Agudo-Canalejo, Jaime1, Author              
Illien, Pierre, Author
Golestanian, Ramin1, Author              
Affiliations:
1Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society, ou_2570692              

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Free keywords: protein complexes; intracellular transport; first passage; reactivity; self-organization
 Abstract: 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 on them a functional advantage with respect to nondissociating 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 nonuniform environments with position-dependent association–dissociation, caused by, for example, 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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Language(s): eng - English
 Dates: 2020-05-15
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Proceedings of the National Academy of Sciences
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 117 (22) Sequence Number: - Start / End Page: 11894 - 11900 Identifier: ISSN: 0027-8424
ISSN: 1091-6490