Evidence map›Paper›PMID 39545739›Full record

ArticleApplied and environmental microbiology2024

ChIP-seq and structural analyses delineating the regulatory mechanism of master regulator EsrB in

Boya Zhang, Yi Zhang, Jingjing Liu, David Reverter, Qiyao Wang, Sang Ho Choi, Bing Liu, Shuai Shao

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Applied and environmental microbiology, 2024. 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

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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. Transcriptional regulatory factorFrontiers in microbiology · 2025
    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

8 authors.

Boya ZhangState Key Laboratory of Bioreactor Engineering, Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, East China University of Science and Technology, Shanghai, China.
Yi ZhangState Key Laboratory of Bioreactor Engineering, Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, East China University of Science and Technology, Shanghai, China.
Jingjing LiuDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China.
David ReverterInstitut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona, Bellaterra, Spain.
Qiyao WangState Key Laboratory of Bioreactor Engineering, Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, East China University of Science and Technology, Shanghai, China.
Sang Ho ChoiNational Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Seoul National University, Seoul, South Korea.ORCID 0000-0003-3865-1039
Bing LiuDepartment of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Hangzhou Normal University, Hangzhou, China.ORCID 0000-0002-6018-998X
Shuai ShaoState Key Laboratory of Bioreactor Engineering, Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, East China University of Science and Technology, Shanghai, China.ORCID 0000-0002-9304-2466

Funding

China Agriculture Research System of MOF and MARA CARS-47Ministerio de Ciencia e Innovación (MCIN) PID2021-124602OB-100MOST | National Key Research and Development Program of China (NKPs) 2022YFE0101200MOST | National Natural Science Foundation of China (NSFC) 32373183
6 · The paper itself

Abstract

As a response regulator of the EsrA-EsrB two-component system, EsrB is conserved in IMPORTANCE: As a crucial virulence regulator, EsrB possesses a LuxR-like superfamily domain at the C-terminal, which is conserved within the canonical NarL family regulators. Due to its critically important role in virulence and pathogenicity in fish hosts, the DNA binding ability has been believed to allow EsrB to regulate genes associated with the invasion process of host cells and basal metabolism in response to environmental stimuli. The lack of EsrB's crystal structure has been a major obstacle in understanding the molecular mechanisms of EsrB-DNA interaction which choreographs EsrB-mediated pathogenic behavior. Here, we conducted ChIP-seq and solved the crystal structure of the C-terminal of EsrB (EsrBC) at 2.20-Å resolution, which revealed that EsrB preferred to bind to virulence-associated promoters with a distinct 7'-4-7' pseudopalindromic DNA motif and interacted with metabolic-related promoters with a high AT DNA motif in Dulbecco's Modified Eagle's Medium (DMEM) (mimicking

Indexed as

Bacterial ProteinsChromatin Immunoprecipitation SequencingEdwardsiellaGene Expression Regulation, BacterialAnimalsEnterobacteriaceae InfectionsFish DiseasesPromoter Regions, GeneticTranscription FactorsVirulenceBacterial ProteinsTranscription FactorsChIP-seqcrystal structureEdwardsiella piscicidaEsrBmetabolismpathogenesis

Identifiers

PMID39545739
PMCPMC11653779

What OpenQuestion 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 OpenQuestion graph.