Structural visualization of key steps in nucleosome reorganization by human FACT

Abstract Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome reorganization conducted by a Mid domai...

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Autores principales:	Kouta Mayanagi, Kazumi Saikusa, Naoyuki Miyazaki, Satoko Akashi, Kenji Iwasaki, Yoshifumi Nishimura, Kosuke Morikawa, Yasuo Tsunaka
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9efebd6a9acf4ca9b718e8a5caa37b29
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spelling	oai:doaj.org-article:9efebd6a9acf4ca9b718e8a5caa37b292021-12-02T15:08:30ZStructural visualization of key steps in nucleosome reorganization by human FACT10.1038/s41598-019-46617-72045-2322https://doaj.org/article/9efebd6a9acf4ca9b718e8a5caa37b292019-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-46617-7https://doaj.org/toc/2045-2322Abstract Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome reorganization conducted by a Mid domain and its adjacent acidic AID segment of human FACT. We determined three cryo-EM structures of respective octasomes complexed with the Mid-AID and AID regions, and a hexasome alone. We discovered extensive contacts between a FACT region and histones H2A, H2B, and H3, suggesting that FACT is competent to direct functional replacement of a nucleosomal DNA end by its phosphorylated AID segment (pAID). Mutational assays revealed that the aromatic and phosphorylated residues within pAID are essential for octasome binding. The EM structure of the hexasome, generated by the addition of Mid-pAID or pAID, indicated that the dissociation of H2A-H2B dimer causes significant alteration from the canonical path of the nucleosomal DNA.Kouta MayanagiKazumi SaikusaNaoyuki MiyazakiSatoko AkashiKenji IwasakiYoshifumi NishimuraKosuke MorikawaYasuo TsunakaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kouta Mayanagi Kazumi Saikusa Naoyuki Miyazaki Satoko Akashi Kenji Iwasaki Yoshifumi Nishimura Kosuke Morikawa Yasuo Tsunaka Structural visualization of key steps in nucleosome reorganization by human FACT
description	Abstract Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome reorganization conducted by a Mid domain and its adjacent acidic AID segment of human FACT. We determined three cryo-EM structures of respective octasomes complexed with the Mid-AID and AID regions, and a hexasome alone. We discovered extensive contacts between a FACT region and histones H2A, H2B, and H3, suggesting that FACT is competent to direct functional replacement of a nucleosomal DNA end by its phosphorylated AID segment (pAID). Mutational assays revealed that the aromatic and phosphorylated residues within pAID are essential for octasome binding. The EM structure of the hexasome, generated by the addition of Mid-pAID or pAID, indicated that the dissociation of H2A-H2B dimer causes significant alteration from the canonical path of the nucleosomal DNA.
format	article
author	Kouta Mayanagi Kazumi Saikusa Naoyuki Miyazaki Satoko Akashi Kenji Iwasaki Yoshifumi Nishimura Kosuke Morikawa Yasuo Tsunaka
author_facet	Kouta Mayanagi Kazumi Saikusa Naoyuki Miyazaki Satoko Akashi Kenji Iwasaki Yoshifumi Nishimura Kosuke Morikawa Yasuo Tsunaka
author_sort	Kouta Mayanagi
title	Structural visualization of key steps in nucleosome reorganization by human FACT
title_short	Structural visualization of key steps in nucleosome reorganization by human FACT
title_full	Structural visualization of key steps in nucleosome reorganization by human FACT
title_fullStr	Structural visualization of key steps in nucleosome reorganization by human FACT
title_full_unstemmed	Structural visualization of key steps in nucleosome reorganization by human FACT
title_sort	structural visualization of key steps in nucleosome reorganization by human fact
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/9efebd6a9acf4ca9b718e8a5caa37b29
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_version_	1718388140299780096

Structural visualization of key steps in nucleosome reorganization by human FACT

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