Evidence map›Paper›PMID 21185190›Full record

ArticleCurrent biology : CB2011

ATP hydrolysis is required for relocating cohesin from sites occupied by its Scc2/4 loading complex.

Bin Hu, Takehiko Itoh, Ajay Mishra, Yuki Katoh, Kok-Lung Chan, William Upcher, Camilla Godlee, Maurici B Roig, Katsuhiko Shirahige, Kim Nasmyth

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

116 citing papers in PubMed, 195 citations in OpenAlex.

  1. Article
  2. Review
  3. NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. DecreasingScience advances · 2022
    Article
  10. Smc5/6 silences episomal transcription by a three-step function.Nature structural & molecular biology · 2022
    Article
  11. DNA sliding and loop formation byBiochemistry and biophysics reports · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Genome folding through loop extrusion by SMC complexes.Nature reviews. Molecular cell biology · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Article

56 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

10 authors at 2 institutions in 2 countries.

Bin Hu *Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Takehiko Itoh *Laboratory of In Silico Functional Genomics, Graduate School of Bioscience, Tokyo Institute of Technology, 4259 Nagatsuta, Midoriku, Yokohama 226-8501, Japan.
Ajay Mishra *Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Yuki KatohLaboratory of In Silico Functional Genomics, Graduate School of Bioscience, Tokyo Institute of Technology, 4259 Nagatsuta, Midoriku, Yokohama 226-8501, Japan.
Kok-Lung ChanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
William UpcherDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Camilla GodleeDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Maurici B RoigDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Katsuhiko ShirahigeLaboratory of In Silico Functional Genomics, Graduate School of Bioscience, Tokyo Institute of Technology, 4259 Nagatsuta, Midoriku, Yokohama 226-8501, Japan.
Kim NasmythDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
University of Oxford · GBTokyo Institute of Technology · JP

Funding

Cancer Research UK 12386Cancer Research UK A6660Wellcome Trust 078241
6 · The paper itself

Abstract

backgroundThe Cohesin complex that holds sister chromatins together until anaphase is comprised of three core subunits: Smc1 and Smc3, two long-rod-shaped proteins with an ABC-like ATPase head (nucleotide-binding domain [NBD]) and a dimerization domain linked by a 50 nm long intramolecular antiparallel coiled-coil, and Scc1, an α-kleisin subunit interconnecting the NBD domains of Smc1 and Smc3. Cohesin's stable association with chromosomes is thought to involve entrapment of chromatin fibers by its tripartite Smc1-Smc3-Scc1 ring via a poorly understood mechanism dependent on a separate Scc2/4 loading complex. A key issue concerns where entrapment initially takes place: at sites where cohesin is found stably associated or at distinct "loading" sites from which it translocates.

resultsIn this study, we find transition state mutant versions (Smc1E1158Q and SmcE1155Q) defective in disengagement of their nucleotide binding domains (NBDs), unlike functional cohesin, colocalize with Scc2/4 at core centromeres, sites that catalyze wild-type cohesin's recruitment to sequences 20 kb or more away. In addition to Scc2/4, the unstable association of transition state complexes with core centromeres requires Scc1's association with Smc1 and Smc3 NBDs, ATP-driven NBD engagement, cohesin's Scc3 subunit, and its hinge domain.

conclusionWe propose that cohesin's association with chromosomes is driven by two key events. NBD engagement driven by ATP binding produces an unstable association with specific loading sites like core centromeres, whereas subsequent ATP hydrolysis triggers DNA entrapment, which permits translocation along chromatin fibers.

Indexed as

Adenosine TriphosphateCell Cycle ProteinsCell DivisionChromatinChromosomal Proteins, Non-HistoneCohesinsGene Expression Regulation, FungalHydrolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsSaccharomyces cerevisiae ProteinsSCC2 protein, S cerevisiaeSCC4 protein, S cerevisiae

Identifiers

PMID21185190
PMCPMC4763544
OpenAlexW2041182908

What OpenQuestion holds

Textmetadata
LicenceTDM
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.