Evidence map›Paper›PMID 37012407›Full record

ArticleNature structural & molecular biology2023

DNA segment capture by Smc5/6 holocomplexes.

Michael Taschner, Stephan Gruber

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  3. Review
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  7. Review
  8. Article
  9. Article
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  11. Article
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  14. In through the out door: A loop-binding-first model for topological cohesin loading.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. 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
  19. Article
  20. SMC-based immunity against extrachromosomal DNA elements.Biochemical Society transactions · 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

2 authors at 1 institution in 1 country.

Michael TaschnerDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-0150-0395
Stephan GruberDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland. stephan.gruber@unil.ch.ORCID http://orcid.org/0000-0002-8881-3705
University of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three distinct structural maintenance of chromosomes (SMC) complexes facilitate chromosome folding and segregation in eukaryotes, presumably by DNA loop extrusion. How SMCs interact with DNA to extrude loops is not well understood. Among the SMC complexes, Smc5/6 has dedicated roles in DNA repair and preventing a buildup of aberrant DNA junctions. In the present study, we describe the reconstitution of ATP-dependent DNA loading by yeast Smc5/6 rings. Loading strictly requires the Nse5/6 subcomplex which opens the kleisin neck gate. We show that plasmid molecules are topologically entrapped in the kleisin and two SMC subcompartments, but not in the full SMC compartment. This is explained by the SMC compartment holding a looped DNA segment and by kleisin locking it in place when passing between the two flanks of the loop for neck-gate closure. Related segment capture events may provide the power stroke in subsequent DNA extrusion steps, possibly also in other SMC complexes, thus providing a unifying principle for DNA loading and extrusion.

Indexed as

Multiprotein ComplexesSaccharomyces cerevisiae ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosomesDNADNA RepairSaccharomyces cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNAMultiprotein ComplexesNSE5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMC5 protein, S cerevisiae

Identifiers

PMID37012407
PMCPMC10191858
OpenAlexW4362521393

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.