Evidence map›Paper›PMID 28238653›Full record

ArticleMolecular cell2017

Tuned SMC Arms Drive Chromosomal Loading of Prokaryotic Condensin.

Frank Bürmann, Alrun Basfeld, Roberto Vazquez Nunez, Marie-Laure Diebold-Durand, Larissa Wilhelm, Stephan Gruber

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
9.1field-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

34 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  8. Motorized chain models of the ideal chromosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Relief of ParB autoinhibition byScience advances · 2021
    Article
  12. Article
  13. Genome folding through loop extrusion by SMC complexes.Nature reviews. Molecular cell biology · 2021
    Review
  14. Article
  15. Article
  16. Review
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  18. Review
  19. Review
  20. Braiding topology and the energy landscape of chromosome organization proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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 2 countries.

Frank BürmannMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Alrun BasfeldMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Roberto Vazquez NunezDepartment of Fundamental Microbiology, University of Lausanne, Bâtiment Biophore, 1015 Lausanne, Switzerland.
Marie-Laure Diebold-DurandMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Larissa WilhelmMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Stephan GruberMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany; Department of Fundamental Microbiology, University of Lausanne, Bâtiment Biophore, 1015 Lausanne, Switzerland. Electronic address: stephan.gruber@unil.ch.
Max Planck Institute of Biochemistry · DEUniversity of Lausanne · CH

Funding

European Research Council 260853
6 · The paper itself

Abstract

SMC proteins support vital cellular processes in all domains of life by organizing chromosomal DNA. They are composed of ATPase "head" and "hinge" dimerization domains and a connecting coiled-coil "arm." Binding to a kleisin subunit creates a closed tripartite ring, whose ∼47-nm-long SMC arms act as barrier for DNA entrapment. Here, we uncover another, more active function of the bacterial Smc arm. Using high-throughput genetic engineering, we resized the arm in the range of 6-60 nm and found that it was functional only in specific length regimes following a periodic pattern. Natural SMC sequences reflect these length constraints. Mutants with improper arm length or peptide insertions in the arm efficiently target chromosomal loading sites and hydrolyze ATP but fail to use ATP hydrolysis for relocation onto flanking DNA. We propose that SMC arms implement force transmission upon nucleotide hydrolysis to mediate DNA capture or loop extrusion.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBacillus subtilisBacterial ProteinsBinding SitesCell Cycle ProteinsChromosomes, BacterialDNA, BacterialDNA-Binding ProteinsGenetic EngineeringHigh-Throughput Screening AssaysHydrolysisMultiprotein ComplexesMutationNucleic Acid ConformationProtein BindingAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCell Cycle Proteinscondensin complexesDNA, BacterialDNA-Binding ProteinsMultiprotein ComplexesSMC protein, Bacteriachromosome segregationcohesincoiled coilcondensinheptad repeatkleisinParBperiodicitySMCSmc/ScpAB

Identifiers

PMID28238653
PMCPMC5344682
OpenAlexW2590164488

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.