Evidence map›Paper›PMID 32930661›Full record

ArticleeLife2020

Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3.

James E Collier, Byung-Gil Lee, Maurici Brunet Roig, Stanislav Yatskevich, Naomi J Petela, Jean Metson, Menelaos Voulgaris, Andres Gonzalez Llamazares, Jan Löwe, Kim A Nasmyth

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.6field-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

53 citing papers in PubMed, 115 citations in OpenAlex.

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  9. 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
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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 1 country.

James E Collier *Department of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID 0000-0002-9904-9423
Byung-Gil Lee *MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0001-9565-6114
Maurici Brunet RoigDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Stanislav YatskevichDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Naomi J PetelaDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Jean MetsonDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Menelaos VoulgarisDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Andres Gonzalez LlamazaresMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0001-5404-6360
Jan LöweMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0002-5218-6615
Kim A NasmythDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID 0000-0001-7030-4403
University of Oxford · GBMRC Laboratory of Molecular Biology · GB

Funding

Cancer Research UK 26747Medical Research Council MC_U105184326Medical Research Council U105184326Wellcome Trust
6 · The paper itself

Abstract

In addition to extruding DNA loops, cohesin entraps within its SMC-kleisin ring (S-K) individual DNAs during G1 and sister DNAs during S-phase. All three activities require related hook-shaped proteins called Scc2 and Scc3. Using thiol-specific crosslinking we provide rigorous proof of entrapment activity in vitro. Scc2 alone promotes entrapment of DNAs in the E-S and E-K compartments, between ATP-bound engaged heads and the SMC hinge and associated kleisin, respectively. This does not require ATP hydrolysis nor is it accompanied by entrapment within S-K rings, which is a slower process requiring Scc3. Cryo-EM reveals that DNAs transported into E-S/E-K compartments are 'clamped' in a sub-compartment created by Scc2's association with engaged heads whose coiled coils are folded around their elbow. We suggest that clamping may be a recurrent feature of cohesin complexes active in loop extrusion and that this conformation precedes the S-K entrapment required for sister chromatid cohesion.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA, FungalModels, MolecularRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA, FungalIRR1 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsSCC2 protein, S cerevisiaebiochemistrychemical biologyCohesinDNA entrapmentS. cerevisiaeSMC

Identifiers

PMID32930661
PMCPMC7492086
OpenAlexW3086608978

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.