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PICH acts as a force-dependent nucleosome remodeler

In anaphase, any unresolved DNA entanglements between the segregating sister chromatids can give rise to chromatin bridges. To prevent genome instability, chromatin bridges must be resolved prior to cytokinesis. The SNF2 protein PICH has been proposed to play a direct role in this process through th...

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Autores principales: Spakman, Dian, Clement, Tinka V. M., Biebricher, Andreas S., King, Graeme A., Singh, Manika I., Hickson, Ian D., Peterman, Erwin J. G., Wuite, Gijs J. L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9700735/
https://www.ncbi.nlm.nih.gov/pubmed/36433994
http://dx.doi.org/10.1038/s41467-022-35040-8
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author Spakman, Dian
Clement, Tinka V. M.
Biebricher, Andreas S.
King, Graeme A.
Singh, Manika I.
Hickson, Ian D.
Peterman, Erwin J. G.
Wuite, Gijs J. L.
author_facet Spakman, Dian
Clement, Tinka V. M.
Biebricher, Andreas S.
King, Graeme A.
Singh, Manika I.
Hickson, Ian D.
Peterman, Erwin J. G.
Wuite, Gijs J. L.
author_sort Spakman, Dian
collection PubMed
description In anaphase, any unresolved DNA entanglements between the segregating sister chromatids can give rise to chromatin bridges. To prevent genome instability, chromatin bridges must be resolved prior to cytokinesis. The SNF2 protein PICH has been proposed to play a direct role in this process through the remodeling of nucleosomes. However, direct evidence of nucleosome remodeling by PICH has remained elusive. Here, we present an in vitro single-molecule assay that mimics chromatin under tension, as is found in anaphase chromatin bridges. Applying a combination of dual-trap optical tweezers and fluorescence imaging of PICH and histones bound to a nucleosome-array construct, we show that PICH is a tension- and ATP-dependent nucleosome remodeler that facilitates nucleosome unwrapping and then subsequently slides remaining histones along the DNA. This work elucidates the role of PICH in chromatin-bridge dissolution, and might provide molecular insights into the mechanisms of related SNF2 proteins.
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spelling pubmed-97007352022-11-27 PICH acts as a force-dependent nucleosome remodeler Spakman, Dian Clement, Tinka V. M. Biebricher, Andreas S. King, Graeme A. Singh, Manika I. Hickson, Ian D. Peterman, Erwin J. G. Wuite, Gijs J. L. Nat Commun Article In anaphase, any unresolved DNA entanglements between the segregating sister chromatids can give rise to chromatin bridges. To prevent genome instability, chromatin bridges must be resolved prior to cytokinesis. The SNF2 protein PICH has been proposed to play a direct role in this process through the remodeling of nucleosomes. However, direct evidence of nucleosome remodeling by PICH has remained elusive. Here, we present an in vitro single-molecule assay that mimics chromatin under tension, as is found in anaphase chromatin bridges. Applying a combination of dual-trap optical tweezers and fluorescence imaging of PICH and histones bound to a nucleosome-array construct, we show that PICH is a tension- and ATP-dependent nucleosome remodeler that facilitates nucleosome unwrapping and then subsequently slides remaining histones along the DNA. This work elucidates the role of PICH in chromatin-bridge dissolution, and might provide molecular insights into the mechanisms of related SNF2 proteins. Nature Publishing Group UK 2022-11-25 /pmc/articles/PMC9700735/ /pubmed/36433994 http://dx.doi.org/10.1038/s41467-022-35040-8 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Spakman, Dian
Clement, Tinka V. M.
Biebricher, Andreas S.
King, Graeme A.
Singh, Manika I.
Hickson, Ian D.
Peterman, Erwin J. G.
Wuite, Gijs J. L.
PICH acts as a force-dependent nucleosome remodeler
title PICH acts as a force-dependent nucleosome remodeler
title_full PICH acts as a force-dependent nucleosome remodeler
title_fullStr PICH acts as a force-dependent nucleosome remodeler
title_full_unstemmed PICH acts as a force-dependent nucleosome remodeler
title_short PICH acts as a force-dependent nucleosome remodeler
title_sort pich acts as a force-dependent nucleosome remodeler
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9700735/
https://www.ncbi.nlm.nih.gov/pubmed/36433994
http://dx.doi.org/10.1038/s41467-022-35040-8
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