Evidence map›Paper›PMID 36881760›Full record

ArticleNucleic acids research2023

The MksG nuclease is the executing part of the bacterial plasmid defense system MksBEFG.

Manuela Weiß, Giacomo Giacomelli, Mathilde Ben Assaya, Finja Grundt, Ahmed Haouz, Feng Peng, Stéphanie Petrella, Anne Marie Wehenkel, Marc Bramkamp

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
10.0field-weighted citation impact, top 2% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. DNA Bioconjugation with Polymer Beads Using SNAP-tag® Technology.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Article
  7. The extended mobility of plasmids.Nucleic acids research · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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

9 authors at 2 institutions in 2 countries.

Manuela WeißInstitute for General Microbiology, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, 24118 Kiel, Germany.
Giacomo GiacomelliInstitute for General Microbiology, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, 24118 Kiel, Germany.
Mathilde Ben AssayaUnité de Microbiologie Structurale, Institut Pasteur, CNRS, Université Paris Cité, 75015 Paris, France.
Finja GrundtInstitute for General Microbiology, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, 24118 Kiel, Germany.
Ahmed HaouzPlate-forme de Cristallographie, C2RT, Institut Pasteur, CNRS UMR 3528, F-75015 Paris, France.
Feng PengInstitute for General Microbiology, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, 24118 Kiel, Germany.
Stéphanie PetrellaUnité de Microbiologie Structurale, Institut Pasteur, CNRS, Université Paris Cité, 75015 Paris, France.
Anne Marie WehenkelUnité de Microbiologie Structurale, Institut Pasteur, CNRS, Université Paris Cité, 75015 Paris, France.
Marc BramkampInstitute for General Microbiology, Christian-Albrechts-University Kiel, Am Botanischen Garten 1-9, 24118 Kiel, Germany.ORCID 0000-0002-7704-3266
Christian-Albrechts-Universität zu Kiel · DECentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells are continuously facing the risk of taking up foreign DNA that can compromise genomic integrity. Therefore, bacteria are in a constant arms race with mobile genetic elements such as phages, transposons and plasmids. They have developed several active strategies against invading DNA molecules that can be seen as a bacterial 'innate immune system'. Here, we investigated the molecular arrangement of the Corynebacterium glutamicum MksBEFG complex, which is homologous to the MukBEF condensin system. We show here that MksG is a nuclease that degrades plasmid DNA. The crystal structure of MksG revealed a dimeric assembly through its C-terminal domain that is homologous to the TOPRIM domain of the topoisomerase II family of enzymes and contains the corresponding ion binding site essential for DNA cleavage in topoisomerases. The MksBEF subunits exhibit an ATPase cycle in vitro and we reason that this reaction cycle, in combination with the nuclease activity provided by MksG, allows for processive degradation of invading plasmids. Super-resolution localization microscopy revealed that the Mks system is spatially regulated via the polar scaffold protein DivIVA. Introduction of plasmids results in an increase in DNA bound MksG, indicating an activation of the system in vivo.

Indexed as

Corynebacterium glutamicumDNA Topoisomerases, Type IIDNA Transposable ElementsGenomePlasmidsDNA Topoisomerases, Type IIDNA Transposable Elements

Identifiers

PMID36881760
PMCPMC10123090
OpenAlexW4323351488

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.