Evidence map›Paper›PMID 25843722›Full record

ArticleCell reports2015

Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.

Younhee Cho, Xin Zhang, Kristine Faye R Pobre, Yu Liu, David L Powers, Jeffery W Kelly, Lila M Gierasch, Evan T Powers

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
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  8. 'Frontiers in microbiology · 2021
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  15. Review
  16. Thermosensitivity of growth is determined by chaperone-mediated proteome reallocation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Article
  19. Bacterial proteostasis balances energy and chaperone utilization efficiently.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

8 authors at 3 institutions in 1 country.

Younhee ChoDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.
Xin ZhangDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.
Kristine Faye R PobreDepartments of Chemistry and Biochemistry and Molecular Biology, University of Massachusetts-Amherst, Amherst, MA 01003, USA.
Yu LiuDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.
David L PowersDepartment of Mathematics and Computer Science, Clarkson University, Potsdam, NY 13699, USA.
Jeffery W KellyDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Lila M GieraschDepartments of Chemistry and Biochemistry and Molecular Biology, University of Massachusetts-Amherst, Amherst, MA 01003, USA. Electronic address: gierasch@biochem.umass.edu.
Evan T PowersDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: epowers@scripps.edu.
Scripps Research Institute · USUniversity of Massachusetts Amherst · USClarkson University · US

Funding

Understanding and Ameliorating Loss-of-Function Protein Misfolding DiseasesR01DK075295 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2006 to 2014
$3.9M
Modeling a cellular protein homeostasis networkR01GM101644 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M, POWERS, EVAN THOMAS · 2013 to 2016
$1.6M
NIDDK NIH HHS DK075295NIDDK NIH HHS R01 DK075295NIGMS NIH HHS GM101644NIGMS NIH HHS R01 GM101644
6 · The paper itself

Abstract

The folding fate of a protein in vivo is determined by the interplay between a protein's folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual components of the E. coli proteostasis network have been studied extensively, but much less is known about how they function as a system. We used an integrated experimental and computational approach to quantitatively analyze the folding outcomes (native folding versus aggregation versus degradation) of three test proteins biosynthesized in E. coli under a variety of conditions. Overexpression of the entire proteostasis network benefited all three test proteins, but the effect of upregulating individual chaperones or the major degradation enzyme, Lon, varied for proteins with different biophysical properties. In sum, the impact of the E. coli proteostasis network is a consequence of concerted action by the Hsp70 system (DnaK/DnaJ/GrpE), the Hsp60 system (GroEL/GroES), and Lon.

Indexed as

Protein FoldingChaperonin 60Escherichia coliEscherichia coli ProteinsHomeostasisHSP70 Heat-Shock ProteinsMolecular ChaperonesProtease LaProtein BiosynthesisProteolysisChaperonin 60Escherichia coli ProteinsHSP70 Heat-Shock ProteinsLon protein, E coliMolecular ChaperonesProtease La

Identifiers

PMID25843722
PMCPMC4401642
OpenAlexW2076603536

What OpenQuestion holds

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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.