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Structural mechanism of extranucleosomal DNA readout by the INO80 complex
The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nucleosome sliding activity that is regulated by ext...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9733932/ https://www.ncbi.nlm.nih.gov/pubmed/36490333 http://dx.doi.org/10.1126/sciadv.add3189 |
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author | Kunert, Franziska Metzner, Felix J. Jung, James Höpfler, Markus Woike, Stephan Schall, Kevin Kostrewa, Dirk Moldt, Manuela Chen, Jia-Xuan Bantele, Susanne Pfander, Boris Eustermann, Sebastian Hopfner, Karl-Peter |
author_facet | Kunert, Franziska Metzner, Felix J. Jung, James Höpfler, Markus Woike, Stephan Schall, Kevin Kostrewa, Dirk Moldt, Manuela Chen, Jia-Xuan Bantele, Susanne Pfander, Boris Eustermann, Sebastian Hopfner, Karl-Peter |
author_sort | Kunert, Franziska |
collection | PubMed |
description | The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nucleosome sliding activity that is regulated by extranucleosomal DNA features. Here, we use cryo–electron microscopy and functional assays to reveal how INO80 binds and is regulated by extranucleosomal DNA. Structures of the regulatory A-module bound to DNA clarify the mechanism of linker DNA binding. The A-module is connected to the motor unit via an HSA/post-HSA lever element to chemomechanically couple the motor and linker DNA sensing. Two notable sites of curved DNA recognition by coordinated action of the four actin/actin-related proteins and the motor suggest how sliding by INO80 can be regulated by extranucleosomal DNA features. Last, the structures clarify the recruitment of YY1/Ies4 subunits and reveal deep architectural similarities between the regulatory modules of INO80 and SWI/SNF complexes. |
format | Online Article Text |
id | pubmed-9733932 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-97339322022-12-14 Structural mechanism of extranucleosomal DNA readout by the INO80 complex Kunert, Franziska Metzner, Felix J. Jung, James Höpfler, Markus Woike, Stephan Schall, Kevin Kostrewa, Dirk Moldt, Manuela Chen, Jia-Xuan Bantele, Susanne Pfander, Boris Eustermann, Sebastian Hopfner, Karl-Peter Sci Adv Biomedicine and Life Sciences The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nucleosome sliding activity that is regulated by extranucleosomal DNA features. Here, we use cryo–electron microscopy and functional assays to reveal how INO80 binds and is regulated by extranucleosomal DNA. Structures of the regulatory A-module bound to DNA clarify the mechanism of linker DNA binding. The A-module is connected to the motor unit via an HSA/post-HSA lever element to chemomechanically couple the motor and linker DNA sensing. Two notable sites of curved DNA recognition by coordinated action of the four actin/actin-related proteins and the motor suggest how sliding by INO80 can be regulated by extranucleosomal DNA features. Last, the structures clarify the recruitment of YY1/Ies4 subunits and reveal deep architectural similarities between the regulatory modules of INO80 and SWI/SNF complexes. American Association for the Advancement of Science 2022-12-09 /pmc/articles/PMC9733932/ /pubmed/36490333 http://dx.doi.org/10.1126/sciadv.add3189 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Kunert, Franziska Metzner, Felix J. Jung, James Höpfler, Markus Woike, Stephan Schall, Kevin Kostrewa, Dirk Moldt, Manuela Chen, Jia-Xuan Bantele, Susanne Pfander, Boris Eustermann, Sebastian Hopfner, Karl-Peter Structural mechanism of extranucleosomal DNA readout by the INO80 complex |
title | Structural mechanism of extranucleosomal DNA readout by the INO80 complex |
title_full | Structural mechanism of extranucleosomal DNA readout by the INO80 complex |
title_fullStr | Structural mechanism of extranucleosomal DNA readout by the INO80 complex |
title_full_unstemmed | Structural mechanism of extranucleosomal DNA readout by the INO80 complex |
title_short | Structural mechanism of extranucleosomal DNA readout by the INO80 complex |
title_sort | structural mechanism of extranucleosomal dna readout by the ino80 complex |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9733932/ https://www.ncbi.nlm.nih.gov/pubmed/36490333 http://dx.doi.org/10.1126/sciadv.add3189 |
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