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Structural Transition of the Nucleosome during Transcription Elongation

In eukaryotes, genomic DNA is tightly wrapped in chromatin. The nucleosome is a basic unit of chromatin, but acts as a barrier to transcription. To overcome this impediment, the RNA polymerase II elongation complex disassembles the nucleosome during transcription elongation. After the RNA polymerase...

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Autores principales: Kujirai, Tomoya, Ehara, Haruhiko, Sekine, Shun-ichi, Kurumizaka, Hitoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10216454/
https://www.ncbi.nlm.nih.gov/pubmed/37408222
http://dx.doi.org/10.3390/cells12101388
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author Kujirai, Tomoya
Ehara, Haruhiko
Sekine, Shun-ichi
Kurumizaka, Hitoshi
author_facet Kujirai, Tomoya
Ehara, Haruhiko
Sekine, Shun-ichi
Kurumizaka, Hitoshi
author_sort Kujirai, Tomoya
collection PubMed
description In eukaryotes, genomic DNA is tightly wrapped in chromatin. The nucleosome is a basic unit of chromatin, but acts as a barrier to transcription. To overcome this impediment, the RNA polymerase II elongation complex disassembles the nucleosome during transcription elongation. After the RNA polymerase II passage, the nucleosome is rebuilt by transcription-coupled nucleosome reassembly. Nucleosome disassembly–reassembly processes play a central role in preserving epigenetic information, thus ensuring transcriptional fidelity. The histone chaperone FACT performs key functions in nucleosome disassembly, maintenance, and reassembly during transcription in chromatin. Recent structural studies of transcribing RNA polymerase II complexed with nucleosomes have provided structural insights into transcription elongation on chromatin. Here, we review the structural transitions of the nucleosome during transcription.
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spelling pubmed-102164542023-05-27 Structural Transition of the Nucleosome during Transcription Elongation Kujirai, Tomoya Ehara, Haruhiko Sekine, Shun-ichi Kurumizaka, Hitoshi Cells Review In eukaryotes, genomic DNA is tightly wrapped in chromatin. The nucleosome is a basic unit of chromatin, but acts as a barrier to transcription. To overcome this impediment, the RNA polymerase II elongation complex disassembles the nucleosome during transcription elongation. After the RNA polymerase II passage, the nucleosome is rebuilt by transcription-coupled nucleosome reassembly. Nucleosome disassembly–reassembly processes play a central role in preserving epigenetic information, thus ensuring transcriptional fidelity. The histone chaperone FACT performs key functions in nucleosome disassembly, maintenance, and reassembly during transcription in chromatin. Recent structural studies of transcribing RNA polymerase II complexed with nucleosomes have provided structural insights into transcription elongation on chromatin. Here, we review the structural transitions of the nucleosome during transcription. MDPI 2023-05-14 /pmc/articles/PMC10216454/ /pubmed/37408222 http://dx.doi.org/10.3390/cells12101388 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kujirai, Tomoya
Ehara, Haruhiko
Sekine, Shun-ichi
Kurumizaka, Hitoshi
Structural Transition of the Nucleosome during Transcription Elongation
title Structural Transition of the Nucleosome during Transcription Elongation
title_full Structural Transition of the Nucleosome during Transcription Elongation
title_fullStr Structural Transition of the Nucleosome during Transcription Elongation
title_full_unstemmed Structural Transition of the Nucleosome during Transcription Elongation
title_short Structural Transition of the Nucleosome during Transcription Elongation
title_sort structural transition of the nucleosome during transcription elongation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10216454/
https://www.ncbi.nlm.nih.gov/pubmed/37408222
http://dx.doi.org/10.3390/cells12101388
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