Evidence map›Paper›PMID 23911325›Full record

ArticleCell2013

Proteotoxic stress induces a cell-cycle arrest by stimulating Lon to degrade the replication initiator DnaA.

Kristina Jonas, Jing Liu, Peter Chien, Michael T Laub

Abstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
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

99 citing papers in PubMed.

  1. Lon protease-mediated secretome profiling inMicrobiology resource announcements · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Cell Fusion and Syncytia Formation in Cancer.Results and problems in cell differentiation · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

39 more citing papers are in PubMed but not listed here.

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

4 authors.

Kristina JonasDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Jing Liu
Peter Chien
Michael T Laub

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Cell Cycle Regulation in Caulobacter CrescentusR01GM082899 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LAUB, MICHAEL · 2008 to 2020
$3.8M
Specificity, Regulation and Proteomic Profiling of an Essential AAA+ ProteaseR00GM084157 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHIEN, PETER · 2010 to 2012
$742k
Howard Hughes Medical InstituteNIGMS NIH HHS 5R01GM082899NIGMS NIH HHS R00 GM084157NIGMS NIH HHS R00GM084157NIGMS NIH HHS R01 GM082899NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

The decision to initiate DNA replication is a critical step in the cell cycle of all organisms. Cells often delay replication in the face of stressful conditions, but the underlying mechanisms remain incompletely defined. Here, we demonstrate in Caulobacter crescentus that proteotoxic stress induces a cell-cycle arrest by triggering the degradation of DnaA, the conserved replication initiator. A depletion of available Hsp70 chaperone, DnaK, either through genetic manipulation or heat shock, induces synthesis of the Lon protease, which can directly degrade DnaA. Unexpectedly, we find that unfolded proteins, which accumulate following a loss of DnaK, also allosterically activate Lon to degrade DnaA, thereby ensuring a cell-cycle arrest. Our work reveals a mechanism for regulating DNA replication under adverse growth conditions. Additionally, our data indicate that unfolded proteins can actively and directly alter substrate recognition by cellular proteases.

Indexed as

DNA ReplicationBacterial ProteinsCaulobacter crescentusDNA, BacterialDNA-Binding ProteinsEscherichia coliHeat-Shock ProteinsHeat-Shock ResponseMolecular ChaperonesProtease LaProtein FoldingSigma FactorStress, PhysiologicalBacterial ProteinsDnaA protein, BacteriaDNA, BacterialDNA-Binding ProteinsHeat-Shock Proteinsheat-shock sigma factor 32Molecular ChaperonesProtease LaSigma Factor

Identifiers

PMID23911325
PMCPMC3749246

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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.