Evidence map›Paper›PMID 25716199›Full record

ArticleOpen biology2015

Three-dimensional topology of the SMC2/SMC4 subcomplex from chicken condensin I revealed by cross-linking and molecular modelling.

Helena Barysz, Ji Hun Kim, Zhuo Angel Chen, Damien F Hudson, Juri Rappsilber, Dietlind L Gerloff, William C Earnshaw

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.0field-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

36 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Mitotic chromosomes.Seminars in cell & developmental biology · 2021
    Review
  6. Quantitative Cross-Linking of Proteins and Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  7. Article
  8. Article
  9. 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
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Development of Large-scale Cross-linking Mass Spectrometry.Molecular & cellular proteomics : MCP · 2018
    Article
  18. Article
  19. Review
  20. 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

7 authors at 4 institutions in 4 countries.

Helena BaryszWellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, UK.
Ji Hun KimWellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, UK Murdoch Children's Research Institute, Royal Children's Hospital, Parkville, Victoria 3052, Australia Department of Paediatrics, University of Melbourne, Parkville, Victoria 3052, Australia.
Zhuo Angel ChenWellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, UK.
Damien F HudsonMurdoch Children's Research Institute, Royal Children's Hospital, Parkville, Victoria 3052, Australia Department of Paediatrics, University of Melbourne, Parkville, Victoria 3052, Australia.
Juri RappsilberWellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, UK Department of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany juri.rappsilber@ed.ac.uk.
Dietlind L GerloffFoundation for Applied Molecular Evolution, PO Box 13174, Gainesville, FL 32604, USA dgerloff@ffame.org.
William C EarnshawWellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, UK bill.earnshaw@ed.ac.uk.
Wellcome Centre for Cell Biology · GBUniversity of Edinburgh · GBFoundation for Applied Molecular Evolution · USMurdoch Children's Research Institute · AU

Funding

Wellcome Trust 073915Wellcome Trust 077707 andWellcome Trust 084229Wellcome Trust 091020Wellcome Trust 092076Wellcome Trust 103139Wellcome Trust 103139/Z/13/Z
6 · The paper itself

Abstract

SMC proteins are essential components of three protein complexes that are important for chromosome structure and function. The cohesin complex holds replicated sister chromatids together, whereas the condensin complex has an essential role in mitotic chromosome architecture. Both are involved in interphase genome organization. SMC-containing complexes are large (more than 650 kDa for condensin) and contain long anti-parallel coiled-coils. They are thus difficult subjects for conventional crystallographic and electron cryomicroscopic studies. Here, we have used amino acid-selective cross-linking and mass spectrometry combined with structure prediction to develop a full-length molecular draft three-dimensional structure of the SMC2/SMC4 dimeric backbone of chicken condensin. We assembled homology-based molecular models of the globular heads and hinges with the lengthy coiled-coils modelled in fragments, using numerous high-confidence cross-links and accounting for potential irregularities. Our experiments reveal that isolated condensin complexes can exist with their coiled-coil segments closely apposed to one another along their lengths and define the relative spatial alignment of the two anti-parallel coils. The centres of the coiled-coils can also approach one another closely in situ in mitotic chromosomes. In addition to revealing structural information, our cross-linking data suggest that both H2A and H4 may have roles in condensin interactions with chromatin.

Indexed as

Models, MolecularAdenosine TriphosphatasesAnimalsCell LineChickensChromosomesDNA-Binding ProteinsGenetic LinkageHistonesMitosisMultiprotein ComplexesNuclear ProteinsProtein ConformationProtein Interaction Domains and MotifsRecombinant Fusion ProteinsAdenosine Triphosphatasescondensin complexesDNA-Binding ProteinsHistonesMultiprotein ComplexesNuclear ProteinsRecombinant Fusion Proteinscoiled-coilcondensincross-linkingmass spectrometrySMCstructure

Identifiers

PMID25716199
PMCPMC4345284
OpenAlexW2147241652

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.