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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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Detalles Bibliográficos
Autores principales: Cutts, Erin E., Vannini, Alessandro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2020
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.
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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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