Evidence map›Paper›PMID 23353789›Full record

ArticleNature structural & molecular biology2013

An asymmetric SMC-kleisin bridge in prokaryotic condensin.

Frank Bürmann, Ho-Chul Shin, Jérôme Basquin, Young-Min Soh, Victor Giménez-Oya, Yeon-Gil Kim, Byung-Ha Oh, Stephan Gruber

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

76 citing papers in PubMed, 138 citations in OpenAlex.

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  10. DNA segment capture by Smc5/6 holocomplexes.Nature structural & molecular biology · 2023
    Article
  11. Form and function of archaeal genomes.Biochemical Society transactions · 2022
    Article
  12. Article
  13. Article
  14. Clamping of DNA shuts the condensin neck gate.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
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  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Frank BürmannMax Planck Research Group Chromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Ho-Chul Shin
Jérôme Basquin
Young-Min Soh
Victor Giménez-Oya
Yeon-Gil Kim
Byung-Ha Oh
Stephan Gruber
Korea Advanced Institute of Science and Technology · KRMax Planck Institute of Biochemistry · DEMax Planck Society · DEPohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form large, ring-shaped assemblies that promote accurate chromosome segregation. Their asymmetric structural core comprises SMC heterodimers that associate with both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is composed of symmetric Smc homodimers associated with the kleisin ScpA in a postulated symmetrical manner. Here, we demonstrate that Smc molecules have two distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled coil, whereas the C terminus binds the Smc ATPase domain. We show that in Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a molecular mechanism that ensures asymmetric assembly, and we conclude that the basic architecture of SMC-kleisin rings evolved before the emergence of eukaryotes.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsBinding SitesCell Cycle ProteinsCross-Linking ReagentsCrystallography, X-RayDNA-Binding ProteinsModels, MolecularMultiprotein ComplexesMutationProtein ConformationProtein MultimerizationProtein Structure, TertiaryStreptococcus pneumoniaeAdenosine TriphosphatasesBacterial ProteinsCell Cycle Proteinscondensin complexesCross-Linking ReagentsDNA-Binding ProteinsMultiprotein ComplexesScpA protein, Bacillus subtilisSMC protein, Bacteria

Identifiers

PMID23353789
OpenAlexW2038178643

What OpenQuestion holds

Textmetadata
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.