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Verfasst von:Winkler, Juliane [VerfasserIn]   i
 Seyberth, Anja [VerfasserIn]   i
 König, Lars [VerfasserIn]   i
 Pruggnaller, Sabine [VerfasserIn]   i
 Haselmann, Uta [VerfasserIn]   i
 Sourjik, Victor [VerfasserIn]   i
 Weiss, Matthias [VerfasserIn]   i
 Frangakis, Achilleas S. [VerfasserIn]   i
 Mogk, Axel [VerfasserIn]   i
 Bukau, Bernd [VerfasserIn]   i
Titel:Quantitative and spatio‐temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
Verf.angabe:Juliane Winkler, Anja Seybert, Lars König, Sabine Pruggnaller, Uta Haselmann, Victor Sourjik, Matthias Weiss, Achilleas S Frangakis, Axel Mogk, Bernd Bukau
E-Jahr:2010
Jahr:21 January 2010
Umfang:14 S.
Illustrationen:Illustrationen
Fussnoten:Gesehen am 26.02.2024
Titel Quelle:Enthalten in: European Molecular Biology OrganizationThe EMBO journal
Ort Quelle:Heidelberg : EMBO Press, 1982
Jahr Quelle:2010
Band/Heft Quelle:29(2010), 5, Seite 910-923
ISSN Quelle:1460-2075
Abstract:The aggregation of proteins as a result of intrinsic or environmental stress may be cytoprotective, but is also linked to pathophysiological states and cellular ageing. We analysed the principles of aggregate formation and the cellular strategies to cope with aggregates in Escherichia coli using fluorescence microscopy of thermolabile reporters, EM tomography and mathematical modelling. Misfolded proteins deposited at the cell poles lead to selective re‐localization of the DnaK/DnaJ/ClpB disaggregating chaperones, but not of GroEL and Lon to these sites. Polar aggregation of cytosolic proteins is mainly driven by nucleoid occlusion and not by an active targeting mechanism. Accordingly, cytosolic aggregation can be efficiently re‐targeted to alternative sites such as the inner membrane in the presence of site‐specific aggregation seeds. Polar positioning of aggregates allows for asymmetric inheritance of damaged proteins, resulting in higher growth rates of damage‐free daughter cells. In contrast, symmetric damage inheritance of randomly distributed aggregates at the inner membrane abrogates this rejuvenation process, indicating that asymmetric deposition of protein aggregates is important for increasing the fitness of bacterial cell populations.
DOI:doi:10.1038/emboj.2009.412
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1038/emboj.2009.412
 Volltext: https://www.embopress.org/doi/full/10.1038/emboj.2009.412
 DOI: https://doi.org/10.1038/emboj.2009.412
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:ageing
 chaperones
 disaggregation
 nucleoid occlusion
 protein aggregation
K10plus-PPN:1881628809
Verknüpfungen:→ Zeitschrift

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