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

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Schlagwörter: protein complexes; intracellular transport; first passage; reactivity; self-organization
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2020-05-152020-06-02
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.1919635117
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 117 (22) Artikelnummer: - Start- / Endseite: 11894 - 11900 Identifikator: ISSN: 0027-8424
ISSN: 1091-6490