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Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones

Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3–H4 chaperones found in distinct and common complexes, yet how...

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Autores principales: Liu, Chao-Pei, Jin, Wenxing, Hu, Jie, Wang, Mingzhu, Chen, Jingjing, Li, Guohong, Xu, Rui-Ming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8653785/
https://www.ncbi.nlm.nih.gov/pubmed/34819355
http://dx.doi.org/10.1101/gad.349100.121
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author Liu, Chao-Pei
Jin, Wenxing
Hu, Jie
Wang, Mingzhu
Chen, Jingjing
Li, Guohong
Xu, Rui-Ming
author_facet Liu, Chao-Pei
Jin, Wenxing
Hu, Jie
Wang, Mingzhu
Chen, Jingjing
Li, Guohong
Xu, Rui-Ming
author_sort Liu, Chao-Pei
collection PubMed
description Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3–H4 chaperones found in distinct and common complexes, yet how sNASP binds H3–H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3–H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3–H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones.
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spelling pubmed-86537852022-06-01 Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones Liu, Chao-Pei Jin, Wenxing Hu, Jie Wang, Mingzhu Chen, Jingjing Li, Guohong Xu, Rui-Ming Genes Dev Research Paper Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3–H4 chaperones found in distinct and common complexes, yet how sNASP binds H3–H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3–H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3–H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones. Cold Spring Harbor Laboratory Press 2021-12-01 /pmc/articles/PMC8653785/ /pubmed/34819355 http://dx.doi.org/10.1101/gad.349100.121 Text en © 2021 Liu et al.; Published by Cold Spring Harbor Laboratory Press https://creativecommons.org/licenses/by-nc/4.0/This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) .
spellingShingle Research Paper
Liu, Chao-Pei
Jin, Wenxing
Hu, Jie
Wang, Mingzhu
Chen, Jingjing
Li, Guohong
Xu, Rui-Ming
Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
title Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
title_full Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
title_fullStr Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
title_full_unstemmed Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
title_short Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
title_sort distinct histone h3–h4 binding modes of snasp reveal the basis for cooperation and competition of histone chaperones
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8653785/
https://www.ncbi.nlm.nih.gov/pubmed/34819355
http://dx.doi.org/10.1101/gad.349100.121
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