Evidence map›Paper›PMID 29175904›Full record

ArticleThe Journal of biological chemistry2018

Cohesin SA2 is a sequence-independent DNA-binding protein that recognizes DNA replication and repair intermediates.

Preston Countryman, Yanlin Fan, Aparna Gorthi, Hai Pan, Evelyn Strickland, Parminder Kaur, Xuechun Wang, Jiangguo Lin, Xiaoying Lei, Christian White and 8 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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
  5. Review
  6. Article
  7. Untangling the loops ofLeukemia & lymphoma · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Function and Evolution of the Loop Extrusion Machinery in Animals.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

18 authors at 8 institutions in 4 countries.

Preston CountrymanFrom the Physics Department.
Yanlin Fanthe Department of BioSciences, Rice University, Houston, Texas 77251.
Aparna Gorthithe Greehey Children's Cancer Research Institute and.
Hai PanFrom the Physics Department.
Evelyn StricklandFrom the Physics Department.
Parminder KaurFrom the Physics Department.
Xuechun WangBiomedical Engineering Department, and.
Jiangguo LinFrom the Physics Department.
Xiaoying Leithe Department of BioSciences, Rice University, Houston, Texas 77251.
Christian WhiteFrom the Physics Department.
Changjiang Youthe Division of Biophysics, Universität Osnabrück, Barbarstrasse 11, 49076 Osnabrück, Germany, and.
Nicolas Wirththe Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Josef-Schneider-Strasse 2, 97080 Würzburg, Germany.
Ingrid Tessmerthe Rudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Josef-Schneider-Strasse 2, 97080 Würzburg, Germany.
Jacob Piehlerthe Division of Biophysics, Universität Osnabrück, Barbarstrasse 11, 49076 Osnabrück, Germany, and.
Robert RiehnFrom the Physics Department.
Alexander J R Bishopthe Greehey Children's Cancer Research Institute and.
Yizhi Jane Taothe Department of BioSciences, Rice University, Houston, Texas 77251.
Hong WangFrom the Physics Department, hong_wang@ncsu.edu.
North Carolina State University · USRice University · USOsnabrück University · DEUniversity of Würzburg · DECentre for Biomedical Engineering and Physics · SEChildren's Cancer Center · USSouth China University of Technology · CNThe University of Texas Health Science Center at San Antonio · US

Funding

Translational Research Support CoreP30ES025128 · NIEHS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI Kelly Sides · 2015 to 2026
$18.3M
Cancer Biology Training ProgramT32CA148724 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Pei Wang, Feng-Chun Yang · 2011 to 2026
$3.3M
Integrative Program in Complex Biological System (ipCBS)T32EB009383 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARSHALL, WALLACE, WEINER, ORION D · 2009 to 2022
$3.2M
Improving etoposide treatment of Ewing's sarcomaR01CA152063 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BISHOP, ALEXANDER JAMES · 2011 to 2015
$1.5M
Mechanism of protein-mediated looping in a complex environmentR01GM107559 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI RIEHN, ROBERT, WANG, HONG · 2014 to 2017
$1.3M
Comparing and contrasting the biology of damage survival at a genomic levelR15ES019128 · NIEHS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BISHOP, ALEXANDER JAMES · 2010 to 2010
$446k
Rotational Tracking of Single Nanoplasmonic Upconverting Nanoparticle-Conjugated Proteins on DNAR21ES027641 · NIEHS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI LIM, SHUANG FANG · 2017 to 2018
$385k
A screen for damage response genes using recombinationK22ES012264 · NIEHS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BISHOP, ALEXANDER JAMES · 2004 to 2006
$321k
NCI NIH HHS R01 CA152063NCI NIH HHS T32 CA148724NIBIB NIH HHS T32 EB009383NIEHS NIH HHS K22 ES012264NIEHS NIH HHS P30 ES025128NIEHS NIH HHS R15 ES019128NIEHS NIH HHS R21 ES027641NIGMS NIH HHS R01 GM107559
6 · The paper itself

Abstract

Proper chromosome alignment and segregation during mitosis depend on cohesion between sister chromatids, mediated by the cohesin protein complex, which also plays crucial roles in diverse genome maintenance pathways. Current models attribute DNA binding by cohesin to entrapment of dsDNA by the cohesin ring subunits (SMC1, SMC3, and RAD21 in humans). However, the biophysical properties and activities of the fourth core cohesin subunit SA2 (STAG2) are largely unknown. Here, using single-molecule atomic force and fluorescence microscopy imaging as well as fluorescence anisotropy measurements, we established that SA2 binds to both dsDNA and ssDNA, albeit with a higher binding affinity for ssDNA. We observed that SA2 can switch between the 1D diffusing (search) mode on dsDNA and stable binding (recognition) mode at ssDNA gaps. Although SA2 does not specifically bind to centromeric or telomeric sequences, it does recognize DNA structures often associated with DNA replication and double-strand break repair, such as a double-stranded end, single-stranded overhang, flap, fork, and ssDNA gap. SA2 loss leads to a defect in homologous recombination-mediated DNA double-strand break repair. These results suggest that SA2 functions at intermediate DNA structures during DNA transactions in genome maintenance pathways. These findings have important implications for understanding the function of cohesin in these pathways.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA-Binding ProteinsDNA RepairDNA ReplicationFluorescence PolarizationGenomic InstabilityMicroscopy, Atomic ForceMicroscopy, FluorescenceProtein BindingCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA-Binding Proteinsatomic force microscopy (AFM)cohesin DNA bindingDNA-binding proteinfluorescence anisotropyfluorescence microscopygenomic instabilityprotein-DNA interactionSA2single-molecule biophysicsSTAG2

Identifiers

PMID29175904
PMCPMC5777247
OpenAlexW2768736041

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.