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Growth-driven displacement of protein aggregates along the cell length ensures partitioning to both daughter cells in Caulobacter crescentus
KTH, School of Engineering Sciences (SCI), Applied Physics, Biophysics.ORCID iD: 0000-0002-3554-9322
KTH, School of Engineering Sciences (SCI), Applied Physics, Biophysics. KTH, Centres, Science for Life Laboratory, SciLifeLab.ORCID iD: 0000-0003-4005-4997
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2019 (English)In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 111, no 6, p. 1430-1448Article in journal (Refereed) Published
Abstract [en]

All living cells must cope with protein aggregation, which occurs as a result of experiencing stress. In previously studied bacteria, aggregated protein is collected at the cell poles and is retained throughout consecutive cell divisions only in old pole-inheriting daughter cells, resulting in aggregation-free progeny within a few generations. In this study, we describe the in vivo kinetics of aggregate formation and elimination following heat and antibiotic stress in the asymmetrically dividing bacterium Caulobacter crescentus. Unexpectedly, in this bacterium, protein aggregates form as multiple distributed foci located throughout the cell volume. Time-lapse microscopy revealed that under moderate stress, the majority of these protein aggregates are short-lived and rapidly dissolved by the major chaperone DnaK and the disaggregase ClpB. Severe stress or genetic perturbation of the protein quality control machinery induces the formation of long-lived aggregates. Importantly, the majority of persistent aggregates neither collect at the cell poles nor are they partitioned to only one daughter cell type. Instead, we show that aggregates are distributed to both daughter cells in the same ratio at each division, which is driven by the continuous elongation of the growing mother cell. Therefore, our study has revealed a new pattern of protein aggregate inheritance in bacteria.

Place, publisher, year, edition, pages
WILEY , 2019. Vol. 111, no 6, p. 1430-1448
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Engineering and Technology
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URN: urn:nbn:se:kth:diva-272455DOI: 10.1111/mmi.14228ISI: 000471131800004PubMedID: 30779464Scopus ID: 2-s2.0-85067254184OAI: oai:DiVA.org:kth-272455DiVA, id: diva2:1425622
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QC 20200421

Available from: 2020-04-21 Created: 2020-04-21 Last updated: 2020-04-21Bibliographically approved

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Alvelid, JonatanTesta, Ilaria

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