Evidence map›Paper›PMID 33849072›Full record

ArticleNucleic acids research2021

Nse5/6 is a negative regulator of the ATPase activity of the Smc5/6 complex.

Stephen T Hallett, Pascale Schellenberger, Lihong Zhou, Fabienne Beuron, Ed Morris, Johanne M Murray, Antony W Oliver

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Allelic Analysis ofInternational journal of molecular sciences · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. In Vitro SUMOylation Assays with a DNA-Sensitive Multi-subunit E3 Ligase.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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
  16. Genome control by SMC complexes.Nature reviews. Molecular cell biology · 2023
    Review
  17. Article
  18. Structural biology of SMC complexes across the tree of life.Current opinion in structural biology · 2023
    Review
  19. Review
  20. DNA segment capture by Smc5/6 holocomplexes.Nature structural & molecular biology · 2023
    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

7 authors at 2 institutions in 1 country.

Stephen T HallettGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, UK.ORCID 0000-0003-3189-3828
Pascale SchellenbergerElectron Microscopy Imaging Centre, School of Life Sciences, University of Sussex, Falmer, UK.ORCID 0000-0002-3719-3120
Lihong ZhouGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, UK.ORCID 0000-0002-8452-4332
Fabienne BeuronThe Institute of Cancer Research, London, UK.ORCID 0000-0003-1513-6181
Ed MorrisThe Institute of Cancer Research, London, UK.ORCID 0000-0003-3544-0041
Johanne M MurrayGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, UK.ORCID 0000-0001-9225-6289
Antony W OliverGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, UK.ORCID 0000-0002-2912-8273
University of Sussex · GBInstitute of Cancer Research · GB

Funding

Medical Research Council G1001668Medical Research Council MR/P018955/1
6 · The paper itself

Abstract

The multi-component Smc5/6 complex plays a critical role in the resolution of recombination intermediates formed during mitosis and meiosis, and in the cellular response to replication stress. Using recombinant proteins, we have reconstituted a series of defined Saccharomyces cerevisiae Smc5/6 complexes, visualised them by negative stain electron microscopy, and tested their ability to function as an ATPase. We find that only the six protein 'holo-complex' is capable of turning over ATP and that its activity is significantly increased by the addition of double-stranded DNA to reaction mixes. Furthermore, stimulation is wholly dependent on functional ATP-binding pockets in both Smc5 and Smc6. Importantly, we demonstrate that budding yeast Nse5/6 acts as a negative regulator of Smc5/6 ATPase activity, binding to the head-end of the complex to suppress turnover, irrespective of the DNA-bound status of the complex.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNAEscherichia coliMicroscopy, Electron, TransmissionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNANSE5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMC5 protein, S cerevisiaeSMC6 protein, S cerevisiae

Identifiers

PMID33849072
PMCPMC8096239
OpenAlexW3129581703

What Socratic 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 Socratic graph.