ArticleNature communications2016
Topology and structure of an engineered human cohesin complex bound to Pds5B.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Motorized chromosome models of mitotic chromosome folding.Nature communications · 2025Article
- 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 · 2025Article
- All eukaryotic SMC proteins induce a twist of -0.6 at each DNA loop extrusion step.Science advances · 2024Article
- Motorized chain models of the ideal chromosome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cohesin-independent STAG proteins interact with RNA and R-loops and promote complex loading.eLife · 2023Article
- Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023Article
- Single-molecule experiments reveal the elbow as an essential folding guide in SMC coiled-coil arms.Biophysical journal · 2022Article
- Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Genome folding through loop extrusion by SMC complexes.Nature reviews. Molecular cell biology · 2021Review
- Integrative analysis reveals unique structural and functional features of the Smc5/6 complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural analysis of histone deacetylase 8 mutants associated with Cornelia de Lange Syndrome spectrum disorders.Journal of structural biology · 2021Article
- SUMO is a pervasive regulator of meiosis.eLife · 2021Article
- Human Condensin I and II Drive Extensive ATP-Dependent Compaction of Nucleosome-Bound DNA.Molecular cell · 2020Article
- Quantifying the heterogeneity of macromolecular machines by mass photometry.Nature communications · 2020Article
- Insights into the energy landscapes of chromosome organization proteins from coevolutionary sequence variation and structural modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Braiding topology and the energy landscape of chromosome organization proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Human cohesin compacts DNA by loop extrusion.Science (New York, N.Y.) · 2019Article
- The Many Roles of Cohesin in Drosophila Gene Transcription.Trends in genetics : TIG · 2019Review
- One protein to rule them all: The role of CCCTC-binding factor in shaping human genome in health and disease.Seminars in cell & developmental biology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cohesin subunits Smc1, Smc3 and Scc1 form large tripartite rings which mediate sister chromatid cohesion and chromatin structure. These are thought to entrap DNA with the help of the associated proteins SA1/2 and Pds5A/B. Structural information is available for parts of cohesin, but analyses of entire cohesin complexes are limited by their flexibility. Here we generated a more rigid 'bonsai' cohesin by truncating the coiled coils of Smc1 and Smc3 and used single-particle electron microscopy, chemical crosslinking-mass spectrometry and in silico modelling to generate three-dimensional models of cohesin bound to Pds5B. The HEAT-repeat protein Pds5B forms a curved structure around the nucleotide-binding domains of Smc1 and Smc3 and bridges the Smc3-Scc1 and SA1-Scc1 interfaces. These results indicate that Pds5B forms an integral part of the cohesin ring by contacting all other cohesin subunits, a property that may reflect the complex role of Pds5 proteins in controlling cohesin-DNA interactions.
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Registered trials
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.