Evidence map›Paper›PMID 30779464›Full record

ArticleMolecular microbiology2019

Growth-driven displacement of protein aggregates along the cell length ensures partitioning to both daughter cells in Caulobacter crescentus.

Frederic D Schramm, Kristen Schroeder, Jonatan Alvelid, Ilaria Testa, Kristina Jonas

Open access · hybridAbstract read
In one paragraph

Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Balance between asymmetric allocation and repair of somatic damage in unicellular life forms as an ancient form of r/K selection.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Applied and environmental microbiology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Nontraditional systems in aging research: an update.Cellular and molecular life sciences : CMLS · 2021
    Review
  17. The Protein Quality Control Network inFrontiers in molecular biosciences · 2021
    Review
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Frederic D SchrammScience for Life Laboratory, Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, 10691, Sweden.ORCID 0000-0003-1858-7770
Kristen SchroederScience for Life Laboratory, Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, 10691, Sweden.ORCID 0000-0002-6271-4530
Jonatan AlvelidScience for Life Laboratory, Department of Applied Physics, KTH Royal Institute of Technology, Stockholm, 10044, Sweden.ORCID 0000-0002-3554-9322
Ilaria TestaScience for Life Laboratory, Department of Applied Physics, KTH Royal Institute of Technology, Stockholm, 10044, Sweden.ORCID 0000-0003-4005-4997
Kristina JonasScience for Life Laboratory, Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, 10691, Sweden.ORCID 0000-0002-1469-4424
Stockholm University · SEScience for Life Laboratory · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Cell DivisionProtein AggregatesAnti-Bacterial AgentsBacterial ProteinsCaulobacter crescentusEndopeptidase ClpHeat-Shock ProteinsHot TemperatureKineticsMolecular ChaperonesStress, PhysiologicalTime-Lapse ImagingAnti-Bacterial AgentsBacterial ProteinsEndopeptidase ClpHeat-Shock ProteinsMolecular ChaperonesProtein Aggregates

Identifiers

PMID30779464
PMCPMC6850343
OpenAlexW2952244809

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.