Evidence map›Paper›PMID 32546830›Full record

ArticleScientific reports2020

A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6.

Lucie Vondrova, Peter Kolesar, Marek Adamus, Matej Nociar, Antony W Oliver, Jan J Palecek

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. The Phenotype ofGenes · 2025
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. DNA segment capture by Smc5/6 holocomplexes.Nature structural & molecular biology · 2023
    Article
  11. Article
  12. Smc5/6 silences episomal transcription by a three-step function.Nature structural & molecular biology · 2022
    Article
  13. Loss of NSE-4 Perturbs Genome Stability and DNA Repair inInternational journal of molecular sciences · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. 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

6 authors at 3 institutions in 2 countries.

Lucie VondrovaNational Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
Peter KolesarNational Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
Marek AdamusMendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
Matej NociarNational Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
Antony W OliverGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton, BN1 9RQ, United Kingdom.
Jan J PalecekNational Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic. jpalecek@sci.muni.cz.
Masaryk University · CZCentral European Institute of Technology – Masaryk University · CZUniversity of Sussex · GB

Funding

Medical Research Council MR/P018955/1
6 · The paper itself

Abstract

The SMC (Structural Maintenance of Chromosomes) complexes are composed of SMC dimers, kleisin and kleisin-interacting (HAWK or KITE) subunits. Mutual interactions of these subunits constitute the basal architecture of the SMC complexes. In addition, binding of ATP molecules to the SMC subunits and their hydrolysis drive dynamics of these complexes. Here, we developed new systems to follow the interactions between SMC5/6 subunits and the relative stability of the complex. First, we show that the N-terminal domain of the Nse4 kleisin molecule binds to the SMC6 neck and bridges it to the SMC5 head. Second, binding of the Nse1 and Nse3 KITE proteins to the Nse4 linker increased stability of the ATP-free SMC5/6 complex. In contrast, binding of ATP to SMC5/6 containing KITE subunits significantly decreased its stability. Elongation of the Nse4 linker partially suppressed instability of the ATP-bound complex, suggesting that the binding of the KITE proteins to the Nse4 linker constrains its limited size. Our data suggest that the KITE proteins may shape the Nse4 linker to fit the ATP-free complex optimally and to facilitate opening of the complex upon ATP binding. This mechanism suggests an important role of the KITE subunits in the dynamics of the SMC5/6 complexes.

Indexed as

Adenosine TriphosphatasesCarrier ProteinsCell Cycle ProteinsMacromolecular SubstancesMutagenesis, Site-DirectedNuclear ProteinsProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AlignmentTwo-Hybrid System TechniquesAdenosine TriphosphatasesCarrier ProteinsCell Cycle ProteinsMacromolecular SubstancesNse1 protein, S pombeNse3 protein, S pombeNse4 protein, S pombeNuclear ProteinsSchizosaccharomyces pombe ProteinsSmc5 protein, S pombesmc6 protein, S pombe

Identifiers

PMID32546830
PMCPMC7297730
OpenAlexW3034254599

What OpenQuestion holds

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LicenceCC BY
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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.