Evidence map›Paper›PMID 34191293›Full record

ArticleThe EMBO journal2021

Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding.

Michael Taschner, Jérôme Basquin, Barbara Steigenberger, Ingmar B Schäfer, Young-Min Soh, Claire Basquin, Esben Lorentzen, Markus Räschle, Richard A Scheltema, Stephan Gruber

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.7field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

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  10. In Vitro SUMOylation Assays with a DNA-Sensitive Multi-subunit E3 Ligase.Methods in molecular biology (Clifton, N.J.) · 2025
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  19. Molecular basis for Nse5-6 mediated regulation of Smc5/6 functions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. 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 5 institutions in 4 countries.

Michael TaschnerDepartment of Fundamental Microbiology (DMF), Faculty of Biology and Medicine (FBM), University of Lausanne (UNIL), Lausanne, Switzerland.ORCID 0000-0002-8881-3705
Jérôme BasquinMax Planck Institute of Biochemistry, Martinsried, Germany.
Barbara SteigenbergerMax Planck Institute of Biochemistry, Martinsried, Germany.
Ingmar B SchäferMax Planck Institute of Biochemistry, Martinsried, Germany.
Young-Min SohDepartment of Fundamental Microbiology (DMF), Faculty of Biology and Medicine (FBM), University of Lausanne (UNIL), Lausanne, Switzerland.
Claire BasquinMax Planck Institute of Biochemistry, Martinsried, Germany.
Esben LorentzenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.ORCID 0000-0001-6493-7220
Markus RäschleMolecular Genetics, University of Kaiserslautern, Kaiserslautern, Germany.
Richard A ScheltemaBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.
Stephan GruberDepartment of Fundamental Microbiology (DMF), Faculty of Biology and Medicine (FBM), University of Lausanne (UNIL), Lausanne, Switzerland.ORCID 0000-0002-0150-0395
Max Planck Institute of Biochemistry · DEUniversity of Lausanne · CHUtrecht University · NLAarhus University · DKUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells employ three SMC (structural maintenance of chromosomes) complexes to control DNA folding and topology. The Smc5/6 complex plays roles in DNA repair and in preventing the accumulation of deleterious DNA junctions. To elucidate how specific features of Smc5/6 govern these functions, we reconstituted the yeast holo-complex. We found that the Nse5/6 sub-complex strongly inhibited the Smc5/6 ATPase by preventing productive ATP binding. This inhibition was relieved by plasmid DNA binding but not by short linear DNA, while opposing effects were observed without Nse5/6. We uncovered two binding sites for Nse5/6 on Smc5/6, based on an Nse5/6 crystal structure and cross-linking mass spectrometry data. One binding site is located at the Smc5/6 arms and one at the heads, the latter likely exerting inhibitory effects on ATP hydrolysis. Cysteine cross-linking demonstrated that the interaction with Nse5/6 anchored the ATPase domains in a non-productive state, which was destabilized by ATP and DNA. Under similar conditions, the Nse4/3/1 module detached from the ATPase. Altogether, we show how DNA substrate selection is modulated by direct inhibition of the Smc5/6 ATPase by Nse5/6.

Indexed as

Adenosine TriphosphateCell Cycle ProteinsChromosomal Proteins, Non-HistoneCryoelectron MicroscopyCrystallography, X-RayDNA, FungalHydrolysisMultiprotein ComplexesProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA, FungalMultiprotein ComplexesNSE5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMC5 protein, S cerevisiaeSMC6 protein, S cerevisiaechromosome segregationcohesioncondensinloop extrusionSmc5/6

Identifiers

PMID34191293
PMCPMC8327961
OpenAlexW3175258067

What OpenQuestion holds

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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.