Evidence map›Paper›PMID 40143738›Full record

ArticleProtein science : a publication of the Protein Society2025

Fine-tuned interactions between globular and disordered regions of single-stranded DNA binding (SSB) protein are required for dynamic condensation under physiological conditions.

Zoltán J Kovács, Péter Ecsédi, Gábor M Harami, János Pálinkás, Mina Botros, Lamiya Mahmudova, Viktoria Katran, Dávid Érfalvy, Miklós Cervenak, László Smeller and 1 more

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Article in Protein science : a publication of the Protein Society, 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

11 authors.

Zoltán J KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Péter EcsédiELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0002-4700-125X
Gábor M HaramiELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0001-7234-2710
János PálinkásELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Mina BotrosELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Lamiya MahmudovaELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Viktoria KatranELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Dávid ÉrfalvyELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Miklós CervenakDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.
László SmellerDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.
Mihály KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.

Funding

Eötvös Loránd University (ELTE) EKÖP-24-4-I-ELTE-184Eötvös Loránd University (ELTE) EKÖP-24-4-II-ELTE-92Eötvös Loránd University (ELTE) KMOP-4.2.1/B-10-2011-0002European Comission, WIDERA 101160233Hungarian Academy of Sciences BO/00566/24HUN-REN Hungarian Research NetworkNational Research, Development and Innovation Office 2018-1.2.1-NKP-2018-00005National Research, Development and Innovation Office ADVANCED150087National Research, Development and Innovation Office K123989National Research, Development and Innovation Office K134595National Research, Development and Innovation Office PD146123National Research, Development and Innovation Office ÚNKP-21-3
6 · The paper itself

Abstract

Increasing evidence points to the importance of liquid-liquid phase separation (LLPS)-driven protein condensation in both eukaryotic and bacterial cell physiology. The formation of condensates may involve interactions between both structured (globular) domains and intrinsically disordered protein regions and requires multivalency that is often brought about by oligomerization. Here we dissect such contributions by assessing engineered variants of bacterial (Escherichia coli) single-stranded DNA binding (SSB) protein whose condensation has recently been implicated in bacterial genome metabolism. A truncated SSB variant (SSBdC, lacking the conserved C-terminal peptide (CTP)) was used to assess the importance of interactions between SSB's globular oligonucleotide/oligosaccharide binding (OB) domain and the CTP. We show that OB-CTP interactions are essential for dynamic condensation in physiological (crowded, glutamate-rich) environments. Via assessment of a protein variant (SSB

Indexed as

DNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsIntrinsically Disordered ProteinsDNA, Single-StrandedDNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsIntrinsically Disordered ProteinsSSB protein, E coligenome maintenanceliquid–liquid phase separation (LLPS)protein–protein interactionssingle‐stranded DNA binding protein (SSB)

Identifiers

PMID40143738
PMCPMC11947617

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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.