Evidence map›Paper›PMID 24358019›Full record

ArticlePLoS biology2013

Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli.

Bentley Lim, Ryoji Miyazaki, Saskia Neher, Deborah A Siegele, Koreaki Ito, Peter Walter, Yoshinori Akiyama, Takashi Yura, Carol A Gross

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 76 citations in OpenAlex.

  1. Comparative Characterization of σInternational journal of molecular sciences · 2026
    Article
  2. Review
  3. Article
  4. Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Mapping direct and indirect MarA/SoxS/Rob/RamA regulons inMicrobiology (Reading, England) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Deletion of Yersinia pestisJournal of bacteriology · 2021
    Article
  12. Article
  13. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Physiological effects of overexpressed sigma factors on fermentative stress response of Zymomonas mobilis.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Article
  20. Protein aggregation in bacteria.FEMS microbiology reviews · 2020
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Bentley LimDepartment of Microbiology and Immunology, University of California at San Francisco, San Francisco, California, United States of America.
Ryoji MiyazakiInstitute for Virus Research, Kyoto University, Kyoto, Japan.
Saskia NeherDepartment of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, California United States of America.
Deborah A SiegeleDepartment of Biology, Texas A&M University, College Station, Texas, United States of America.
Koreaki ItoFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Peter WalterDepartment of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, California United States of America.
Yoshinori AkiyamaInstitute for Virus Research, Kyoto University, Kyoto, Japan.
Takashi YuraFaculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Carol A GrossDepartment of Microbiology and Immunology, University of California at San Francisco, San Francisco, California, United States of America ; Department of Cell and Tissue Biology, University of California at San Francisco, San Francisco, California, United States.
Howard Hughes Medical Institute · USKyoto Sangyo University · JPKyoto University · JPUniversity of California, San Francisco · USTexas A&M University · US

Funding

REGULATION OF THE HEAT-SHOCK RESPONSE IN E COLIR01GM036278 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI GROSS, CAROL ANNE · 1986 to 2016
$5.2M
REGULATION OF THE HEAT SHOCK RESPONSE IN E. COLIR37GM036278 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI GROSS, CAROL ANNE · 1995 to 2004
$2.0M
NIGMS NIH HHS GM-36278NIGMS NIH HHS R01 GM036278NIGMS NIH HHS R37 GM036278
6 · The paper itself

Abstract

All cells must adapt to rapidly changing conditions. The heat shock response (HSR) is an intracellular signaling pathway that maintains proteostasis (protein folding homeostasis), a process critical for survival in all organisms exposed to heat stress or other conditions that alter the folding of the proteome. Yet despite decades of study, the circuitry described for responding to altered protein status in the best-studied bacterium, E. coli, does not faithfully recapitulate the range of cellular responses in response to this stress. Here, we report the discovery of the missing link. Surprisingly, we found that σ(32), the central transcription factor driving the HSR, must be localized to the membrane rather than dispersed in the cytoplasm as previously assumed. Genetic analyses indicate that σ(32) localization results from a protein targeting reaction facilitated by the signal recognition particle (SRP) and its receptor (SR), which together comprise a conserved protein targeting machine and mediate the cotranslational targeting of inner membrane proteins to the membrane. SRP interacts with σ(32) directly and transports it to the inner membrane. Our results show that σ(32) must be membrane-associated to be properly regulated in response to the protein folding status in the cell, explaining how the HSR integrates information from both the cytoplasm and bacterial cell membrane.

Indexed as

Bacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsHomeostasisProtein FoldingSigma FactorSignal Recognition ParticleBacterial Outer Membrane ProteinsEscherichia coli ProteinsHeat-Shock Proteinsheat-shock sigma factor 32Sigma FactorSignal Recognition Particle

Identifiers

PMID24358019
PMCPMC3866087
OpenAlexW2080489532

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.