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Topology and structure of an engineered human cohesin complex bound to Pds5B
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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4996973/ https://www.ncbi.nlm.nih.gov/pubmed/27549742 http://dx.doi.org/10.1038/ncomms12523 |
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author | Hons, Michael T. Huis in ‘t Veld, Pim J. Kaesler, Jan Rombaut, Pascaline Schleiffer, Alexander Herzog, Franz Stark, Holger Peters, Jan-Michael |
author_facet | Hons, Michael T. Huis in ‘t Veld, Pim J. Kaesler, Jan Rombaut, Pascaline Schleiffer, Alexander Herzog, Franz Stark, Holger Peters, Jan-Michael |
author_sort | Hons, Michael T. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4996973 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-49969732016-09-07 Topology and structure of an engineered human cohesin complex bound to Pds5B Hons, Michael T. Huis in ‘t Veld, Pim J. Kaesler, Jan Rombaut, Pascaline Schleiffer, Alexander Herzog, Franz Stark, Holger Peters, Jan-Michael Nat Commun Article 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. Nature Publishing Group 2016-08-23 /pmc/articles/PMC4996973/ /pubmed/27549742 http://dx.doi.org/10.1038/ncomms12523 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Hons, Michael T. Huis in ‘t Veld, Pim J. Kaesler, Jan Rombaut, Pascaline Schleiffer, Alexander Herzog, Franz Stark, Holger Peters, Jan-Michael Topology and structure of an engineered human cohesin complex bound to Pds5B |
title | Topology and structure of an engineered human cohesin complex bound to Pds5B |
title_full | Topology and structure of an engineered human cohesin complex bound to Pds5B |
title_fullStr | Topology and structure of an engineered human cohesin complex bound to Pds5B |
title_full_unstemmed | Topology and structure of an engineered human cohesin complex bound to Pds5B |
title_short | Topology and structure of an engineered human cohesin complex bound to Pds5B |
title_sort | topology and structure of an engineered human cohesin complex bound to pds5b |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4996973/ https://www.ncbi.nlm.nih.gov/pubmed/27549742 http://dx.doi.org/10.1038/ncomms12523 |
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