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• W2115570853 abstract "Protein misfolding and aggregation are inevitable but detrimental cellular processes. Cells therefore possess protein quality control mechanisms based on chaperones and proteases that (re)fold or hydrolyze unfolded, misfolded, and aggregated proteins. Besides these conserved quality control mechanisms, the spatial organization of protein aggregates (PAs) inside the cell has been proposed as an important additional strategy to deal with their cytotoxicity. In the bacterium Escherichia coli, however, it remained unclear how this spatial organization is established and how this process of assembling PAs in the cell poles affects cellular physiology. In this report, high hydrostatic pressure was used to transiently reverse protein aggregation in living E. coli cells, allowing the subsequent (re)assembly of PAs to be studied in detail. This approach revealed PA assembly to be dependent on intracellular energy and metabolic activity, with the resulting PA structure being confined to the cell pole by nucleoid occlusion. Moreover, a correlation could be observed between the time needed for PA reassembly and the individual lag time of the cells, which might prevent symmetric segregation of cytotoxic PAs among siblings to occur and ensure rapid spatial clearance of molecular damage throughout the emerging population." @default.
• W2115570853 created "2016-06-24" @default.
• W2115570853 creator A5017217582 @default.
• W2115570853 creator A5030124638 @default.
• W2115570853 creator A5063140185 @default.
• W2115570853 date "2014-07-01" @default.
• W2115570853 modified "2023-10-12" @default.
• W2115570853 title "<i>In Vivo</i> Disassembly and Reassembly of Protein Aggregates in Escherichia coli" @default.
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• W2115570853 doi "https://doi.org/10.1128/jb.01549-14" @default.
• W2115570853 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4054163" @default.
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• W2115570853 hasPublicationYear "2014" @default.
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