Evidence map›Paper›PMID 40100851›Full record

ArticleCell reports2025

Uncovering the mechanism for polar sequestration of the major bacterial sugar regulator by high-throughput screens and 3D interaction modeling.

Nitsan Albocher-Kedem, Meta Heidenreich, Amir Fadel, Elizabeta Sirotkin, Omer Goldberger, Anat Nussbaum-Shochat, Emmanuel D Levy, Ora Schueler-Furman, Maya Schuldiner, Orna Amster-Choder

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Article in Cell reports, 2025. 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
–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

2 citing papers in PubMed.

  1. Article
  2. 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

10 authors.

Nitsan Albocher-KedemDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel.
Meta HeidenreichDepartment of Chemical and Structural Biology, The Weizmann Institute of Science, Rehovot 7610001, Israel.
Amir FadelDepartment of Molecular Genetics, The Weizmann Institute of Science, Rehovot 7610001, Israel.
Elizabeta SirotkinDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel.
Omer GoldbergerDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel.
Anat Nussbaum-ShochatDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel.
Emmanuel D LevyDepartment of Chemical and Structural Biology, The Weizmann Institute of Science, Rehovot 7610001, Israel; Department of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Ora Schueler-FurmanDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel.
Maya SchuldinerDepartment of Molecular Genetics, The Weizmann Institute of Science, Rehovot 7610001, Israel.
Orna Amster-ChoderDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel. Electronic address: ornaam@ekmd.huji.ac.il.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The poles of rod-shaped bacteria emerge as regulatory hubs. We have shown that enzyme I (EI), the major bacterial sugar metabolism regulator, is sequestered when not needed in TmaR phase-separated condensates in Escherichia coli cell poles. Here, we combined genetic and automated microscopy screens to identify residues in EI and TmaR that are important for their interaction and colocalization. Mutating these residues affects EI-TmaR interaction in bacteria and impairs co-phase separation in yeast. The results were used to generate an EI-TmaR interaction model, which agrees with coevolution data and is supported by conservation of the interacting residues and EI-TmaR colocalization in other species. Mutating residues predicted to interact electrostatically further supports our model. The model explains how TmaR controls EI activity and its interaction with the phosphoprotein HPr and, hence, sugar uptake. Our study highlights the importance of sugar metabolism spatial regulation during evolution and presents a way to unravel protein-protein interactions.

Indexed as

Escherichia coliEscherichia coli ProteinsHigh-Throughput Screening AssaysPhosphoenolpyruvate Sugar Phosphotransferase SystemSugarsModels, MolecularProtein BindingEscherichia coli ProteinsPhosphoenolpyruvate Sugar Phosphotransferase SystemSugars3D interaction modelingbacterial cell polesCP: MicrobiologyCP: Molecular biologyenzyme I, EIhigh-throughput screensphase separation, PSprotein-protein interactionPTSsubcellular localization in bacteriaTmaR

Identifiers

PMID40100851
PMCPMC11937232

What Socratic holds

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Registered trials

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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 Socratic graph.