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Recent advances in cohesin biology

Sister chromatids are tethered together from the time they are formed in S-phase until they separate at anaphase. A protein complex called cohesin is responsible for holding the sister chromatids together and serves important roles in chromosome condensation, gene regulation, and the repair of DNA d...

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Autores principales: Rankin, Susannah, Dawson, Dean S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: F1000Research 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4975370/
https://www.ncbi.nlm.nih.gov/pubmed/27547382
http://dx.doi.org/10.12688/f1000research.8881.1
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author Rankin, Susannah
Dawson, Dean S.
author_facet Rankin, Susannah
Dawson, Dean S.
author_sort Rankin, Susannah
collection PubMed
description Sister chromatids are tethered together from the time they are formed in S-phase until they separate at anaphase. A protein complex called cohesin is responsible for holding the sister chromatids together and serves important roles in chromosome condensation, gene regulation, and the repair of DNA damage. Cohesin contains an open central pore and becomes topologically engaged with its DNA substrates. Entrapped DNA can be released either by the opening of a gate in the cohesin ring or by proteolytic cleavage of a component of the ring. This review summarizes recent research that provides important new insights into how DNA enters and exits the cohesin ring and how the rings behave on entrapped DNA molecules to provide functional cohesion.
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spelling pubmed-49753702016-08-18 Recent advances in cohesin biology Rankin, Susannah Dawson, Dean S. F1000Res Review Sister chromatids are tethered together from the time they are formed in S-phase until they separate at anaphase. A protein complex called cohesin is responsible for holding the sister chromatids together and serves important roles in chromosome condensation, gene regulation, and the repair of DNA damage. Cohesin contains an open central pore and becomes topologically engaged with its DNA substrates. Entrapped DNA can be released either by the opening of a gate in the cohesin ring or by proteolytic cleavage of a component of the ring. This review summarizes recent research that provides important new insights into how DNA enters and exits the cohesin ring and how the rings behave on entrapped DNA molecules to provide functional cohesion. F1000Research 2016-08-03 /pmc/articles/PMC4975370/ /pubmed/27547382 http://dx.doi.org/10.12688/f1000research.8881.1 Text en Copyright: © 2016 Rankin S and Dawson DS http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Rankin, Susannah
Dawson, Dean S.
Recent advances in cohesin biology
title Recent advances in cohesin biology
title_full Recent advances in cohesin biology
title_fullStr Recent advances in cohesin biology
title_full_unstemmed Recent advances in cohesin biology
title_short Recent advances in cohesin biology
title_sort recent advances in cohesin biology
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4975370/
https://www.ncbi.nlm.nih.gov/pubmed/27547382
http://dx.doi.org/10.12688/f1000research.8881.1
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