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Condensin complexes: understanding loop extrusion one conformational change at a time
Condensin and cohesin, both members of the structural maintenance of chromosome (SMC) family, contribute to the regulation and structure of chromatin. Recent work has shown both condensin and cohesin extrude DNA loops and most likely work via a conserved mechanism. This review focuses on condensin c...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7609036/ https://www.ncbi.nlm.nih.gov/pubmed/33005926 http://dx.doi.org/10.1042/BST20200241 |
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author | Cutts, Erin E. Vannini, Alessandro |
author_facet | Cutts, Erin E. Vannini, Alessandro |
author_sort | Cutts, Erin E. |
collection | PubMed |
description | Condensin and cohesin, both members of the structural maintenance of chromosome (SMC) family, contribute to the regulation and structure of chromatin. Recent work has shown both condensin and cohesin extrude DNA loops and most likely work via a conserved mechanism. This review focuses on condensin complexes, highlighting recent in vitro work characterising DNA loop formation and protein structure. We discuss similarities between condensin and cohesin complexes to derive a possible mechanistic model, as well as discuss differences that exist between the different condensin isoforms found in higher eukaryotes. |
format | Online Article Text |
id | pubmed-7609036 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-76090362020-11-06 Condensin complexes: understanding loop extrusion one conformational change at a time Cutts, Erin E. Vannini, Alessandro Biochem Soc Trans Review Articles Condensin and cohesin, both members of the structural maintenance of chromosome (SMC) family, contribute to the regulation and structure of chromatin. Recent work has shown both condensin and cohesin extrude DNA loops and most likely work via a conserved mechanism. This review focuses on condensin complexes, highlighting recent in vitro work characterising DNA loop formation and protein structure. We discuss similarities between condensin and cohesin complexes to derive a possible mechanistic model, as well as discuss differences that exist between the different condensin isoforms found in higher eukaryotes. Portland Press Ltd. 2020-10-30 2020-10-02 /pmc/articles/PMC7609036/ /pubmed/33005926 http://dx.doi.org/10.1042/BST20200241 Text en © 2020 The Author(s) https://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Articles Cutts, Erin E. Vannini, Alessandro Condensin complexes: understanding loop extrusion one conformational change at a time |
title | Condensin complexes: understanding loop extrusion one conformational change at a time |
title_full | Condensin complexes: understanding loop extrusion one conformational change at a time |
title_fullStr | Condensin complexes: understanding loop extrusion one conformational change at a time |
title_full_unstemmed | Condensin complexes: understanding loop extrusion one conformational change at a time |
title_short | Condensin complexes: understanding loop extrusion one conformational change at a time |
title_sort | condensin complexes: understanding loop extrusion one conformational change at a time |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7609036/ https://www.ncbi.nlm.nih.gov/pubmed/33005926 http://dx.doi.org/10.1042/BST20200241 |
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