ArticleBiophysical journal2014
In vivo kinetics of segregation and polar retention of MS2-GFP-RNA complexes in Escherichia coli.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.Chemical reviews · 2024Review
- Confinement anisotropy drives polar organization of two DNA molecules interacting in a nanoscale cavity.Nature communications · 2022Article
- Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022Review
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- Growth-driven displacement of protein aggregates along the cell length ensures partitioning to both daughter cells in Caulobacter crescentus.Molecular microbiology · 2019Article
- Protein polarization driven by nucleoid exclusion of DnaK(HSP70)-substrate complexes.Nature communications · 2018Article
- Division-Based, Growth Rate Diversity in Bacteria.Frontiers in microbiology · 2018Article
- Polar Localization of the Serine Chemoreceptor of Escherichia coli Is Nucleoid Exclusion-Dependent.Biophysical journal · 2016Article
- Robustness of the Process of Nucleoid Exclusion of Protein Aggregates in Escherichia coli.Journal of bacteriology · 2016Article
- In silico analysis of division times of Escherichia coli populations as a function of the partitioning scheme of non-functional proteins.In silico biology · 2015Article
- Cytoplasmic dynamics reveals two modes of nucleoid-dependent mobility.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoplasm of Escherichia coli is a crowded, heterogeneous environment. From single cell live imaging, we investigated the spatial kinetics and heterogeneities of synthetic RNA-protein complexes. First, although their known tendency to accumulate at the cell poles does not appear to introduce asymmetries between older and newer cell poles within a cell lifetime, these emerge with cell divisions. This suggests strong polar retention of the complexes, which we verified in their history of positions and mean escape time from the poles. Next, we show that the polar retention relies on anisotropies in the displacement distribution in the region between midcell and poles, whereas the speed is homogeneous along the major cell axis. Afterward, we establish that these regions are at the border of the nucleoid and shift outward with cell growth, due to the nucleoid's replication. Overall, the spatiotemporal kinetics of the complexes, which is robust to suboptimal temperatures, suggests that nucleoid occlusion is a source of dynamic heterogeneities of macromolecules in E. coli that ultimately generate phenotypic differences between sister cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.