Evidence map›Paper›PMID 36533901›Full record

ArticleeLife2022

Structures of RecBCD in complex with phage-encoded inhibitor proteins reveal distinctive strategies for evasion of a bacterial immunity hub.

Martin Wilkinson, Oliver J Wilkinson, Connie Feyerherm, Emma E Fletcher, Dale B Wigley, Mark S Dillingham

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. Review
  5. Review
  6. Structural basis for Lamassu-based antiviral immunity and its evolution from DNA repair machinery.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. mLife · 2024
    Review
  16. Article
  17. Review
  18. Article
  19. RecBCD enzyme: mechanistic insights from mutants of a complex helicase-nuclease.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  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

6 authors at 2 institutions in 1 country.

Martin WilkinsonSection of Structural Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0001-5490-613X
Oliver J WilkinsonDNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0003-4107-6434
Connie FeyerhermDNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom.
Emma E FletcherDNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom.
Dale B WigleySection of Structural Biology, Department of Infectious Disease, Faculty of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0002-0786-6726
Mark S DillinghamDNA:protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-4612-7141
University of Bristol · GBImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S007261/1Cancer Research UK 12799Cancer Research UK C6913/A2160Medical Research Council MR/N009258/1Medical Research Council MR/R009023/1Wellcome Trust 100401/Z/12/ZWellcome Trust 209327/Z/17/Z
6 · The paper itself

Abstract

Following infection of bacterial cells, bacteriophage modulate double-stranded DNA break repair pathways to protect themselves from host immunity systems and prioritise their own recombinases. Here, we present biochemical and structural analysis of two phage proteins, gp5.9 and Abc2, which target the DNA break resection complex RecBCD. These exemplify two contrasting mechanisms for control of DNA break repair in which the RecBCD complex is either inhibited or co-opted for the benefit of the invading phage. Gp5.9 completely inhibits RecBCD by preventing it from binding to DNA. The RecBCD-gp5.9 structure shows that gp5.9 acts by substrate mimicry, binding predominantly to the RecB arm domain and competing sterically for the DNA binding site. Gp5.9 adopts a parallel coiled-coil architecture that is unprecedented for a natural DNA mimic protein. In contrast, binding of Abc2 does not substantially affect the biochemical activities of isolated RecBCD. The RecBCD-Abc2 structure shows that Abc2 binds to the Chi-recognition domains of the RecC subunit in a position that might enable it to mediate the loading of phage recombinases onto its single-stranded DNA products.

Indexed as

BacteriophagesEscherichia coli ProteinsAzidesCystineDNADNA, BacterialDNA, Single-StrandedEscherichia coliExodeoxyribonucleasesExodeoxyribonuclease VRecombinasesAzidesCystineDNADNA, BacterialDNA, Single-StrandedEscherichia coli ProteinsExodeoxyribonucleasesExodeoxyribonuclease VN,N'-bis(4-azidobenzoyl)cystineRecombinasesbacterial immunitybacteriophagebiochemistrychemical biologyDNA break repairE. colihelicasemolecular biophysicsRecBCDstructural biology

Identifiers

PMID36533901
PMCPMC9836394
OpenAlexW4311931795

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.