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Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis

Canonical histone H3.1 and variant H3.3 deposit at different sites of the chromatin via distinct histone chaperones. Histone H3.1 relies on chaperone CAF-1 to mediate replication-dependent nucleosome assembly during S-phase, while H3.3 variant is regulated and incorporated into the chromatin in a re...

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Detalles Bibliográficos
Autores principales: Wen, Ting, Chen, Qiao Yi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8786718/
https://www.ncbi.nlm.nih.gov/pubmed/35087762
http://dx.doi.org/10.3389/fonc.2021.806974
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author Wen, Ting
Chen, Qiao Yi
author_facet Wen, Ting
Chen, Qiao Yi
author_sort Wen, Ting
collection PubMed
description Canonical histone H3.1 and variant H3.3 deposit at different sites of the chromatin via distinct histone chaperones. Histone H3.1 relies on chaperone CAF-1 to mediate replication-dependent nucleosome assembly during S-phase, while H3.3 variant is regulated and incorporated into the chromatin in a replication-independent manner through HIRA and DAXX/ATRX. Current literature suggests that dysregulated expression of histone chaperones may be implicated in tumor progression. Notably, ectopic expression of CAF-1 can promote a switch between canonical H3.1 and H3 variants in the chromatin, impair the chromatic state, lead to chromosome instability, and impact gene transcription, potentially contributing to carcinogenesis. This review focuses on the chaperone proteins of H3.1 and H3.3, including structure, regulation, as well as their oncogenic and tumor suppressive functions in tumorigenesis.
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spelling pubmed-87867182022-01-26 Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis Wen, Ting Chen, Qiao Yi Front Oncol Oncology Canonical histone H3.1 and variant H3.3 deposit at different sites of the chromatin via distinct histone chaperones. Histone H3.1 relies on chaperone CAF-1 to mediate replication-dependent nucleosome assembly during S-phase, while H3.3 variant is regulated and incorporated into the chromatin in a replication-independent manner through HIRA and DAXX/ATRX. Current literature suggests that dysregulated expression of histone chaperones may be implicated in tumor progression. Notably, ectopic expression of CAF-1 can promote a switch between canonical H3.1 and H3 variants in the chromatin, impair the chromatic state, lead to chromosome instability, and impact gene transcription, potentially contributing to carcinogenesis. This review focuses on the chaperone proteins of H3.1 and H3.3, including structure, regulation, as well as their oncogenic and tumor suppressive functions in tumorigenesis. Frontiers Media S.A. 2022-01-11 /pmc/articles/PMC8786718/ /pubmed/35087762 http://dx.doi.org/10.3389/fonc.2021.806974 Text en Copyright © 2022 Wen and Chen https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Oncology
Wen, Ting
Chen, Qiao Yi
Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
title Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
title_full Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
title_fullStr Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
title_full_unstemmed Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
title_short Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
title_sort dynamic activity of histone h3-specific chaperone complexes in oncogenesis
topic Oncology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8786718/
https://www.ncbi.nlm.nih.gov/pubmed/35087762
http://dx.doi.org/10.3389/fonc.2021.806974
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