Evidence map›Paper›PMID 40128403›Full record

ArticleExtremophiles : life under extreme conditions2025

Adapting to salinity: structural dynamics of the DNA polymerase III beta subunit in Salinibacter ruber.

Aveepsa Sengupta, Dhrubajyoti Das, Anisha Debnath, Yusuf Akhter, Ashutosh Kumar

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Article in Extremophiles : life under extreme conditions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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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

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Aveepsa SenguptaMicrobial Adaptation Laboratory, Department of Microbiology, Tripura University (A Central University), Agartala, Tripura, 799022, India.
Dhrubajyoti DasMicrobial Adaptation Laboratory, Department of Microbiology, Tripura University (A Central University), Agartala, Tripura, 799022, India.
Anisha DebnathMicrobial Adaptation Laboratory, Department of Microbiology, Tripura University (A Central University), Agartala, Tripura, 799022, India.
Yusuf AkhterDepartment of Biotechnology, Babasaheb Bhimrao Ambedkar University, Vidya Vihar, Raebareli Road, Lucknow, Uttar Pradesh, 226025, India. yusuf@daad-alumni.de.ORCID http://orcid.org/0000-0001-9564-9790
Ashutosh KumarMicrobial Adaptation Laboratory, Department of Microbiology, Tripura University (A Central University), Agartala, Tripura, 799022, India. ashutoshkumar@tripurauniv.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Halophilic bacteria thrive in high-salt environments through structural modifications in their proteins. One such adaptation is seen in the DNA polymerase III beta subunit, which acts as a "sliding clamp" for the DNA polymerase III, the replication machinery's key enzyme. Like other halophilic proteins, DNA Pol III beta of Salinibacter ruber displays an increased concentration of acidic amino acids, intrinsically disordered regions, and a negatively charged surface. A detailed study using interaction and molecular dynamics simulations analyses unveils the structural intricacies of S. ruber's beta subunit dimer at the molecular level. The elliptical shape of the dimer facilitates its efficient loading onto DNA in salty environments. Modifications in the dimer enable the DNA loading-unloading mechanism by stabilizing the dimeric conformation at high salt concentrations. Additionally, the study sheds light on the molecular-level conformational changes in the interfaces of the Pol III beta subunit.

Indexed as

Bacterial ProteinsBacteroidetesDNA Polymerase IIISalinityMolecular Dynamics SimulationBacterial Proteinsbeta subunit, DNA polymerase IIIDNA Polymerase IIIDNA Polymerase III betaHalophilesReplicationSalinibacter ruberSalt-dependent adaptations

Identifiers

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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.