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Oocyte-specific linker histone H1foo interacts with Esrrb to induce chromatin decondensation at specific gene loci.

Authors :
Hayakawa, Koji
Tanaka, Satoshi
Source :
Biochemical & Biophysical Research Communications. Jul2021, Vol. 561, p165-171. 7p.
Publication Year :
2021

Abstract

Linker histone H1 is mainly localized in the linker DNA region, between two nucleosome cores, and regulates chromatin structures linking gene expression. Mammalian oocytes contain the histone H1foo, a distinct member with low sequence similarity to other members in the H1 histone family. Although, from various previous studies, evidence related to H1foo function in chromatin structures is being accumulated, the distribution of H1foo at the target gene loci in a genome-wide manner and the molecular mechanism of H1foo-dependent chromatin architecture remain unclear. In this study, we aimed to identify the target loci and the physiological factor bound to H1foo at the loci. Chromatin immunoprecipitation sequencing analysis of H1foo-overexpressing mouse embryonic stem cells showed that H1foo is enriched around the transcriptional start sites of genes such as oocyte-specific genes and that the chromatin structures at these regions were relaxed. We demonstrated that H1foo was physiologically bound to the nuclear receptor estrogen-related receptor beta (Esrrb), and Esrrb was necessary for H1foo activity of chromatin decondensation at the target loci. The specific localization and interaction with Esrrb were validated in endogenous H1foo of oocytes. Overall, H1foo induces chromatin decondensation in a locus-specific manner and this function is achieved by interacting with Esrrb. • H1foo is located at specific target loci including oocyte-specific genes. • H1foo induces chromatin relaxation at specific loci. • H1foo physiologically binds with Esrrb and is co-localized at specific loci. • H1foo induces chromatin relaxation upon binding with Esrrb. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0006291X
Volume :
561
Database :
Academic Search Index
Journal :
Biochemical & Biophysical Research Communications
Publication Type :
Academic Journal
Accession number :
150613614
Full Text :
https://doi.org/10.1016/j.bbrc.2021.05.033