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Nucleosome dynamics during chromatin remodeling in vivo

Precise positioning of nucleosomes around regulatory sites is achieved by the action of chromatin remodelers, which use the energy of ATP to slide, evict or change the composition of nucleosomes. Chromatin remodelers act to bind nucleosomes, disrupt histone-DNA interactions and translocate the DNA a...

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Detalles Bibliográficos
Autores principales: Ramachandran, Srinivas, Henikoff, Steven
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4916871/
https://www.ncbi.nlm.nih.gov/pubmed/26933790
http://dx.doi.org/10.1080/19491034.2016.1149666
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author Ramachandran, Srinivas
Henikoff, Steven
author_facet Ramachandran, Srinivas
Henikoff, Steven
author_sort Ramachandran, Srinivas
collection PubMed
description Precise positioning of nucleosomes around regulatory sites is achieved by the action of chromatin remodelers, which use the energy of ATP to slide, evict or change the composition of nucleosomes. Chromatin remodelers act to bind nucleosomes, disrupt histone-DNA interactions and translocate the DNA around the histone core to reposition nucleosomes. Hence, remodeling is expected to involve nucleosomal intermediates with a structural organization that is distinct from intact nucleosomes. We describe the identification of a partially unwrapped nucleosome structure using methods that map histone-DNA contacts genome-wide. This alternative nucleosome structure is likely formed as an intermediate or by-product during nucleosome remodeling by the RSC complex. Identification of the loss of histone-DNA contacts during chromatin remodeling by RSC in vivo has implications for the regulation of transcriptional initiation.
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spelling pubmed-49168712016-07-06 Nucleosome dynamics during chromatin remodeling in vivo Ramachandran, Srinivas Henikoff, Steven Nucleus Extra View Precise positioning of nucleosomes around regulatory sites is achieved by the action of chromatin remodelers, which use the energy of ATP to slide, evict or change the composition of nucleosomes. Chromatin remodelers act to bind nucleosomes, disrupt histone-DNA interactions and translocate the DNA around the histone core to reposition nucleosomes. Hence, remodeling is expected to involve nucleosomal intermediates with a structural organization that is distinct from intact nucleosomes. We describe the identification of a partially unwrapped nucleosome structure using methods that map histone-DNA contacts genome-wide. This alternative nucleosome structure is likely formed as an intermediate or by-product during nucleosome remodeling by the RSC complex. Identification of the loss of histone-DNA contacts during chromatin remodeling by RSC in vivo has implications for the regulation of transcriptional initiation. Taylor & Francis 2016-03-02 /pmc/articles/PMC4916871/ /pubmed/26933790 http://dx.doi.org/10.1080/19491034.2016.1149666 Text en © 2016 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted
spellingShingle Extra View
Ramachandran, Srinivas
Henikoff, Steven
Nucleosome dynamics during chromatin remodeling in vivo
title Nucleosome dynamics during chromatin remodeling in vivo
title_full Nucleosome dynamics during chromatin remodeling in vivo
title_fullStr Nucleosome dynamics during chromatin remodeling in vivo
title_full_unstemmed Nucleosome dynamics during chromatin remodeling in vivo
title_short Nucleosome dynamics during chromatin remodeling in vivo
title_sort nucleosome dynamics during chromatin remodeling in vivo
topic Extra View
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4916871/
https://www.ncbi.nlm.nih.gov/pubmed/26933790
http://dx.doi.org/10.1080/19491034.2016.1149666
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