Evidence map›Paper›PMID 35199390›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2022

Allosteric differences dictate GroEL complementation of E. coli.

Jared Sivinski, Duc Ngo, Christopher J Zerio, Andrew J Ambrose, Edmond R Watson, Lynn K Kaneko, Marius M Kostelic, Mckayla Stevens, Anne-Marie Ray, Yangshin Park and 7 more

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 54% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
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

17 authors at 4 institutions in 1 country.

Jared SivinskiDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.ORCID https://orcid.org/0000-0003-2696-6279
Duc NgoDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
Christopher J ZerioDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
Andrew J AmbroseDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
Edmond R WatsonDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA.
Lynn K KanekoDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
Marius M KostelicDepartment of Chemistry and Biochemistry, The University of Arizona, Tucson, Arizona, USA.
Mckayla StevensDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Anne-Marie RayDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Yangshin ParkDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Chunxiang WuDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.
Michael T MartyDepartment of Chemistry and Biochemistry, The University of Arizona, Tucson, Arizona, USA.
Quyen Q HoangDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Donna D ZhangDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA.
Steven M JohnsonDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.ORCID https://orcid.org/0000-0001-7254-4128
Eli ChapmanDepartment of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
University of Arizona · USIndiana University School of MedicineScripps Institution of Oceanography · USYale University · US

Funding

CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008804 · NIGMS · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2003 to 2023
$3.9M
Unravelling Membrane Protein-Lipid Interactions using Nanodiscs and Mass SpectrometryR35GM128624 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Michael T Marty · 2018 to 2026
$3.6M
Selective modulation of bacterial chaperonins by targeting novel small molecule binding sitesR01GM120350 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI JOHNSON, STEVEN MICHAEL · 2017 to 2021
$2.3M
Molecular bases of leucine rich repeat kinase 2 activity regulationR01GM115844 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI HOANG, QUYEN QUOC, YUE, ZHENYU · 2016 to 2019
$2.2M
Structure and Function of the Parkinson's disease associated protein LRRK2R01GM111639 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI HOANG, QUYEN QUOC · 2015 to 2019
$1.6M
NIGMS NIH HHS R01 GM111639NIGMS NIH HHS R01 GM115844NIGMS NIH HHS R01 GM120350NIGMS NIH HHS R35 GM128624NIGMS NIH HHS T32 GM008804
6 · The paper itself

Abstract

GroES/GroEL is the only bacterial chaperone essential under all conditions, making it a potential antibiotic target. Rationally targeting ESKAPE GroES/GroEL as an antibiotic strategy necessitates studying their structure and function. Herein, we outline the structural similarities between Escherichia coli and ESKAPE GroES/GroEL and identify significant differences in intra- and inter-ring cooperativity, required in the refolding cycle of client polypeptides. Previously, we observed that one-half of ESKAPE GroES/GroEL family members could not support cell viability when each was individually expressed in GroES/GroEL-deficient E. coli cells. Cell viability was found to be dependent on the allosteric compatibility between ESKAPE and E. coli subunits within mixed (E. coli and ESKAPE) tetradecameric GroEL complexes. Interestingly, differences in allostery did not necessarily result in differences in refolding rate for a given homotetradecameric chaperonin. Characterization of ESKAPE GroEL allostery, ATPase, and refolding rates in this study will serve to inform future studies focused on inhibitor design and mechanism of action studies.

Indexed as

Allosteric SiteAdenosine DiphosphateAdenosine TriphosphateAllosteric RegulationChaperonin 10Escherichia coliEscherichia coli ProteinsHeat-Shock ProteinsProtein SubunitsAdenosine DiphosphateAdenosine TriphosphateChaperonin 10Escherichia coli ProteinsGroE protein, E coliHeat-Shock ProteinsProtein SubunitsallosterychaperonechaperoninESKAPEGroELGroES

Identifiers

PMID35199390
PMCPMC8887798
OpenAlexW4213447383

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.