Evidence map›Paper›PMID 27644322›Full record

ArticleeLife2016

Mechanism for nuclease regulation in RecBCD.

Martin Wilkinson, Yuriy Chaban, Dale B Wigley

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. The RecBC complex protects single-stranded DNA gaps during lesion bypass.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. RecBCD enzyme: mechanistic insights from mutants of a complex helicase-nuclease.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  11. Article
  12. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. The CRISPR-associated Cas4 protein fromCurrent research in microbial sciences · 2021
    Article
  15. Article
  16. Clutch mechanism of chemomechanical coupling in a DNA resecting motor nuclease.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Frontiers in bioengineering and biotechnology · 2021
    Article
  19. 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

3 authors.

Martin WilkinsonSection of Structural Biology, Department of Medicine, Imperial College London, London, United Kingdom.
Yuriy ChabanSection of Structural Biology, Department of Medicine, Imperial College London, London, United Kingdom.
Dale B WigleySection of Structural Biology, Department of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0002-0786-6726

Funding

Cancer Research UK 12799Cancer Research UK A21608Medical Research Council MR/N009258/1Wellcome Trust 095519
6 · The paper itself

Abstract

In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly processive, duplex unwinding and degrading machines that require tight regulation. Here, we report the structure of E.coli RecBCD, determined by cryoEM at 3.8 Å resolution, with a DNA substrate that reveals how the nuclease activity of the complex is activated once unwinding progresses. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains and, to our knowledge, this is the first example of peptide-binding of an SH3 domain in a bacterial system.

Indexed as

Cryoelectron MicroscopyDNAEscherichia coliExodeoxyribonuclease VModels, MolecularProtein ConformationDNAExodeoxyribonuclease VbiophysicschromosomesDNA repairE. coligeneshomologous recombinationRecBCDstructural biology

Identifiers

PMID27644322
PMCPMC5030088

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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.