Evidence map›Paper›PMID 25951515›Full record

ArticleeLife2015

SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis.

Larissa Wilhelm, Frank Bürmann, Anita Minnen, Ho-Chul Shin, Christopher P Toseland, Byung-Ha Oh, Stephan Gruber

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
15.8field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
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  7. Physical models of bacterial chromosomes.Molecular microbiology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. DNA segment capture by Smc5/6 holocomplexes.Nature structural & molecular biology · 2023
    Article
  15. Article
  16. Article
  17. DNA sliding and loop formation byBiochemistry and biophysics reports · 2022
    Article
  18. Smc5/6 silences episomal transcription by a three-step function.Nature structural & molecular biology · 2022
    Article
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

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 at 3 institutions in 2 countries.

Larissa WilhelmChromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Frank BürmannChromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Anita MinnenChromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Ho-Chul ShinDepartment of Biological Sciences, KAIST Institute for the Biocentury, Cancer Metastasis Control Center, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.
Christopher P ToselandChromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Byung-Ha OhDepartment of Biological Sciences, KAIST Institute for the Biocentury, Cancer Metastasis Control Center, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.
Stephan GruberChromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Max Planck Institute of Biochemistry · DEKorea Advanced Institute of Science and Technology · KRKorea Research Institute of Bioscience and Biotechnology · KR

Funding

European Research Council 260853
6 · The paper itself

Abstract

Smc-ScpAB forms elongated, annular structures that promote chromosome segregation, presumably by compacting and resolving sister DNA molecules. The mechanistic basis for its action, however, is only poorly understood. Here, we have established a physical assay to determine whether the binding of condensin to native chromosomes in Bacillus subtilis involves entrapment of DNA by the Smc-ScpAB ring. To do so, we have chemically cross-linked the three ring interfaces in Smc-ScpAB and thereafter isolated intact chromosomes under protein denaturing conditions. Exclusively species of Smc-ScpA, which were previously cross-linked into covalent rings, remained associated with chromosomal DNA. DNA entrapment is abolished by mutations that interfere with the Smc ATPase cycle and strongly reduced when the recruitment factor ParB is deleted, implying that most Smc-ScpAB is loaded onto the chromosome at parS sites near the replication origin. We furthermore report a physical interaction between native Smc-ScpAB and chromosomal DNA fragments.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBacillus subtilisBacterial ProteinsCell Cycle ProteinsChromosomes, BacterialDNA, BacterialDNA-Binding ProteinsHydrolysisMultiprotein ComplexesAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCell Cycle Proteinscondensin complexesDNA, BacterialDNA-Binding ProteinsMultiprotein ComplexesSMC protein, BacteriabiochemistryB. subtilischromosome condensationchromosomeschromosome segregationcondensingenesParB proteinsliding clampSmc proteins

Identifiers

PMID25951515
PMCPMC4442127
OpenAlexW2148216513

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.