Evidence map›Paper›PMID 40770054›Full record

ArticleCommunications biology2025

Filamentation-driven peripheral clustering of the inducible lysine decarboxylase is crucial for E. coli acid stress response.

Moritz A Kirchner, Jessica El Khoury, Frédéric Barras, Jean-Philippe Kleman, Irina Gutsche

Abstract read
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

5 authors.

Moritz A KirchnerInstitut de Biologie Structurale, CEA, CNRS UMR5075, Univ Grenoble Alpes, Grenoble, France.
Jessica El KhouryDepartment of Microbiology, Institut Pasteur, Université de Paris, CNRS UMR6047, Stress Adaptation and Metabolism Unit, Paris, France.
Frédéric BarrasDepartment of Microbiology, Institut Pasteur, Université de Paris, CNRS UMR6047, Stress Adaptation and Metabolism Unit, Paris, France.
Jean-Philippe KlemanInstitut de Biologie Structurale, CEA, CNRS UMR5075, Univ Grenoble Alpes, Grenoble, France. jean-philippe.kleman@ibs.fr.ORCID http://orcid.org/0000-0001-5648-5295
Irina GutscheInstitut de Biologie Structurale, CEA, CNRS UMR5075, Univ Grenoble Alpes, Grenoble, France. irina.gutsche@ibs.fr.ORCID http://orcid.org/0000-0002-1908-3921

Funding

EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 647784
6 · The paper itself

Abstract

Bacteria use sophisticated acid stress response strategies to withstand fluctuating environmental pH, with enterobacterial inducible amino acid decarboxylases playing a major role. The lysine decarboxylase LdcI catalyses lysine-to-cadaverine conversion coupled to proton consumption and carbon dioxide release, thereby buffering cytoplasmic and extracellular pH. Our previous studies showed that Escherichia coli LdcI forms intracellular patches under mild acid stress, and that purified LdcI polymerises into filaments at acidic pH. Here, we investigated the physiological relevance of LdcI filamentation using 3D super-resolution microscopy and an LdcI polymerisation-deficient E. coli mutant strain. We established a semi-automated workflow for intracellular cluster detection and quantitative analysis, and demonstrated predominantly peripheral clustering of LdcI. Disrupting LdcI polymerisation markedly reduced cluster size without significantly affecting localisation, suggesting that clustering is driven by filamentation. Growth and pH measurements revealed that the mutant exhibits reduced fitness and impaired extracellular buffering compared to the wild type, indicating that LdcI polymerisation enhances the E. coli capacity to counteract acid stress without affecting intracellular location of the enzyme. Our findings provide strong evidence that LdcI filamentation regulates acid stress response by spatially optimising enzymatic activity. More broadly, this work supports the functional significance of metabolic enzyme self-assembly in bacterial stress adaptation.

Indexed as

AcidsCarboxy-LyasesEscherichia coliEscherichia coli ProteinsStress, PhysiologicalHydrogen-Ion ConcentrationMutationAcidsCarboxy-LyasesEscherichia coli Proteinslysine decarboxylase

Identifiers

PMID40770054
PMCPMC12328647

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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.