Evidence map›Paper›PMID 38511671›Full record

ArticleProtein science : a publication of the Protein Society2024

DNA-dependent phase separation by human SSB2 (NABP1/OBFC2A) protein points to adaptations to eukaryotic genome repair processes.

Zoltán J Kovács, Gábor M Harami, János Pálinkás, Natalie Kuljanishvili, József Hegedüs, Hajnalka Harami-Papp, Lamiya Mahmudova, Lana Khamisi, Gergely Szakács, Mihály Kovács

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 32% of its field
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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

10 authors at 2 institutions in 2 countries.

Zoltán J KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
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.
Natalie KuljanishviliELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
József HegedüsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Hajnalka Harami-PappELTE-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.
Lana KhamisiELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Gergely SzakácsHUN-REN Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Mihály KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.ORCID 0000-0002-1200-4741
Eötvös Loránd University · HUComprehensive Cancer Center Vienna · AT

Funding

HUN-REN Hungarian Research Network 01055Innovációs és Technológiai Minisztérium Co-operative_Doctoral_ProgramInnovációs és Technológiai Minisztérium "SzintPlusz"_Thematic_Excellence_ProgrammeInnovációs és Technológiai Minisztérium ÚNKP-19-2Innovációs és Technológiai Minisztérium ÚNKP-21-3Magyar Tudományos Akadémia LP2011-006/2011Magyar Tudományos Akadémia PREMIUM-2017-17Nemzeti Kutatási Fejlesztési és Innovációs Hivatal 2018-1.2.1-NKP-2018-00005Nemzeti Kutatási Fejlesztési és Innovációs Hivatal ELTE_KMOP-4.2.1/B-10-2011-0002Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K-123989Nemzeti Kutatási Fejlesztési és Innovációs Hivatal K-134595
6 · The paper itself

Abstract

Single-stranded DNA binding proteins (SSBs) are ubiquitous across all domains of life and play essential roles via stabilizing and protecting single-stranded (ss) DNA as well as organizing multiprotein complexes during DNA replication, recombination, and repair. Two mammalian SSB paralogs (hSSB1 and hSSB2 in humans) were recently identified and shown to be involved in various genome maintenance processes. Following our recent discovery of the liquid-liquid phase separation (LLPS) propensity of Escherichia coli (Ec) SSB, here we show that hSSB2 also forms LLPS condensates under physiologically relevant ionic conditions. Similar to that seen for EcSSB, we demonstrate the essential contribution of hSSB2's C-terminal intrinsically disordered region (IDR) to condensate formation, and the selective enrichment of various genome metabolic proteins in hSSB2 condensates. However, in contrast to EcSSB-driven LLPS that is inhibited by ssDNA binding, hSSB2 phase separation requires single-stranded nucleic acid binding, and is especially facilitated by ssDNA. Our results reveal an evolutionarily conserved role for SSB-mediated LLPS in the spatiotemporal organization of genome maintenance complexes. At the same time, differential LLPS features of EcSSB and hSSB2 point to functional adaptations to prokaryotic versus eukaryotic genome metabolic contexts.

Indexed as

DNAPhase SeparationAnimalsDNA-Binding ProteinsDNA RepairDNA ReplicationDNA, Single-StrandedEscherichia coliHumansMammalsDNADNA-Binding ProteinsDNA, Single-StrandedDNA repairhSSB2liquid–liquid phase separationLLPSNABP1OBFC2Areplicationsingle‐stranded DNA binding proteinSOSSB2

Identifiers

PMID38511671
PMCPMC10955726
OpenAlexW4393042626

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.