Evidence map›Paper›PMID 40168993›Full record

ArticleCell2025

Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic.

Frank Bürmann, Bryony Clifton, Sophie Koekemoer, Oliver J Wilkinson, Dari Kimanius, Mark S Dillingham, Jan Löwe

Abstract read
In one paragraph

Article in Cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. 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.

Frank BürmannMRC Laboratory of Molecular Biology, Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK; University of Oxford, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, UK. Electronic address: frank.burmann@bioch.ox.ac.uk.
Bryony CliftonUniversity of Bristol, School of Biochemistry, DNA:Protein Interactions Unit, Bristol BS8 1TD, UK.
Sophie KoekemoerUniversity of Bristol, School of Biochemistry, DNA:Protein Interactions Unit, Bristol BS8 1TD, UK.
Oliver J WilkinsonUniversity of Bristol, School of Biochemistry, DNA:Protein Interactions Unit, Bristol BS8 1TD, UK.
Dari KimaniusMRC Laboratory of Molecular Biology, Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK; CZ Imaging Institute, 3400 Bridge Parkway, Redwood City, CA 94065, USA.
Mark S DillinghamUniversity of Bristol, School of Biochemistry, DNA:Protein Interactions Unit, Bristol BS8 1TD, UK. Electronic address: mark.dillingham@bristol.ac.uk.
Jan LöweMRC Laboratory of Molecular Biology, Structural Studies, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: jyl@mrc-lmb.cam.ac.uk.

Funding

Medical Research Council MC_U105184326Wellcome Trust
6 · The paper itself

Abstract

Ring-like structural maintenance of chromosome (SMC) complexes are crucial for genome organization and operate through mechanisms of DNA entrapment and loop extrusion. Here, we explore the DNA loading process of the bacterial SMC complex MukBEF. Using cryoelectron microscopy (cryo-EM), we demonstrate that ATP binding opens one of MukBEF's three potential DNA entry gates, exposing a DNA capture site that positions DNA at the open neck gate. We discover that the gp5.9 protein of bacteriophage T7 blocks this capture site by DNA mimicry, thereby preventing DNA loading and inactivating MukBEF. We propose a comprehensive and unidirectional loading mechanism in which DNA is first captured at the complex's periphery and then ingested through the DNA entry gate, powered by a single cycle of ATP hydrolysis. These findings illuminate a fundamental aspect of how ubiquitous DNA organizers are primed for genome maintenance and demonstrate how this process can be disrupted by viruses.

Indexed as

Bacterial ProteinsChromosomal Proteins, Non-HistoneDNADNA, ViralAdenosine TriphosphateBacteriophage T7Cryoelectron MicroscopyDNA, BacterialEscherichia coliViral ProteinsAdenosine TriphosphateBacterial ProteinsChromosomal Proteins, Non-HistoneDNADNA, BacterialDNA, ViralViral Proteinsbacteriophagescohesincondensincryo-EMDNA mimicsMukBEFSMC complexesWadjet

Identifiers

PMID40168993
PMCPMC7617805

What OpenQuestion holds

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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.