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Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome

ATP-dependent chromatin remodeling factors of SWI/SNF2 family including ISWI, SNF2, CHD1 and INO80 subfamilies share a conserved but functionally non-interchangeable ATPase domain. Here we report cryo-electron microscopy (cryo-EM) structures of the nucleosome bound to an ISWI fragment with deletion...

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Autores principales: Chittori, Sagar, Hong, Jingjun, Bai, Yawen, Subramaniam, Sriram
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6755096/
https://www.ncbi.nlm.nih.gov/pubmed/31402386
http://dx.doi.org/10.1093/nar/gkz670
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author Chittori, Sagar
Hong, Jingjun
Bai, Yawen
Subramaniam, Sriram
author_facet Chittori, Sagar
Hong, Jingjun
Bai, Yawen
Subramaniam, Sriram
author_sort Chittori, Sagar
collection PubMed
description ATP-dependent chromatin remodeling factors of SWI/SNF2 family including ISWI, SNF2, CHD1 and INO80 subfamilies share a conserved but functionally non-interchangeable ATPase domain. Here we report cryo-electron microscopy (cryo-EM) structures of the nucleosome bound to an ISWI fragment with deletion of the AutoN and HSS regions in nucleotide-free conditions and the free nucleosome at ∼ 4 Å resolution. In the bound conformation, the ATPase domain interacts with the super helical location 2 (SHL 2) of the nucleosomal DNA, with the N-terminal tail of H4 and with the α1 helix of H3. Density for other regions of ISWI is not observed, presumably due to disorder. Comparison with the structure of the free nucleosome reveals that although the histone core remains largely unchanged, remodeler binding causes perturbations in the nucleosomal DNA resulting in a bulge near the SHL2 site. Overall, the structure of the nucleotide-free ISWI-nucleosome complex is similar to the corresponding regions of the recently reported ADP bound ISWI-nucleosome structures, which are significantly different from that observed for the ADP-BeFx bound structure. Our findings are relevant to the initial step of ISWI binding to the nucleosome and provide additional insights into the nucleosome remodeling process driven by ISWI.
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spelling pubmed-67550962019-09-26 Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome Chittori, Sagar Hong, Jingjun Bai, Yawen Subramaniam, Sriram Nucleic Acids Res Structural Biology ATP-dependent chromatin remodeling factors of SWI/SNF2 family including ISWI, SNF2, CHD1 and INO80 subfamilies share a conserved but functionally non-interchangeable ATPase domain. Here we report cryo-electron microscopy (cryo-EM) structures of the nucleosome bound to an ISWI fragment with deletion of the AutoN and HSS regions in nucleotide-free conditions and the free nucleosome at ∼ 4 Å resolution. In the bound conformation, the ATPase domain interacts with the super helical location 2 (SHL 2) of the nucleosomal DNA, with the N-terminal tail of H4 and with the α1 helix of H3. Density for other regions of ISWI is not observed, presumably due to disorder. Comparison with the structure of the free nucleosome reveals that although the histone core remains largely unchanged, remodeler binding causes perturbations in the nucleosomal DNA resulting in a bulge near the SHL2 site. Overall, the structure of the nucleotide-free ISWI-nucleosome complex is similar to the corresponding regions of the recently reported ADP bound ISWI-nucleosome structures, which are significantly different from that observed for the ADP-BeFx bound structure. Our findings are relevant to the initial step of ISWI binding to the nucleosome and provide additional insights into the nucleosome remodeling process driven by ISWI. Oxford University Press 2019-09-26 2019-08-12 /pmc/articles/PMC6755096/ /pubmed/31402386 http://dx.doi.org/10.1093/nar/gkz670 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Structural Biology
Chittori, Sagar
Hong, Jingjun
Bai, Yawen
Subramaniam, Sriram
Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome
title Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome
title_full Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome
title_fullStr Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome
title_full_unstemmed Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome
title_short Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosome
title_sort structure of the primed state of the atpase domain of chromatin remodeling factor iswi bound to the nucleosome
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6755096/
https://www.ncbi.nlm.nih.gov/pubmed/31402386
http://dx.doi.org/10.1093/nar/gkz670
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