Other formats:
BibTeX
LaTeX
RIS
@article{2248089,
author = {Legartova, Sona and Lochmanová, Gabriela and Bartova, Eva},
article_location = {SWITZERLAND},
article_number = {6},
doi = {http://dx.doi.org/10.3390/life12060798},
keywords = {histone H1; histone H3; chromatin; epigenetic; nucleolus; mass spectrometry},
language = {eng},
issn = {2075-1729},
journal = {LIFE-BASEL},
title = {The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation},
url = {https://www.mdpi.com/2075-1729/12/6/798},
volume = {12},
year = {2022}
}
TY - JOUR
ID - 2248089
AU - Legartova, Sona - Lochmanová, Gabriela - Bartova, Eva
PY - 2022
TI - The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation
JF - LIFE-BASEL
VL - 12
IS - 6
SP - 798
EP - 798
PB - MDPI
SN - 20751729
KW - histone H1
KW - histone H3
KW - chromatin
KW - epigenetic
KW - nucleolus
KW - mass spectrometry
UR - https://www.mdpi.com/2075-1729/12/6/798
N2 - Background: Variants of linker histone H1 are tissue-specific and are responsible for chromatin compaction accompanying cell differentiation, mitotic chromosome condensation, and apoptosis. Heterochromatinization, as the main feature of these processes, is also associated with pronounced trimethylation of histones H3 at the lysine 9 position (H3K9me3). Methods: By confocal microscopy, we analyzed cell cycle-dependent levels and distribution of phosphorylated histone H1 (H1ph) and H3K9me3. By mass spectrometry, we studied post-translational modifications of linker histones. Results: Phosphorylated histone H1, similarly to H3K9me3, has a comparable level in the G1, S, and G2 phases of the cell cycle. A high density of phosphorylated H1 was inside nucleoli of mouse embryonic stem cells (ESCs). H1ph was also abundant in prophase and prometaphase, while H1ph was absent in anaphase and telophase. H3K9me3 surrounded chromosomal DNA in telophase. This histone modification was barely detectable in the early phases of mitosis. Mass spectrometry revealed several ESC-specific phosphorylation sites of H1. HDAC1 depletion did not change H1 acetylation but potentiated phosphorylation of H1.2/H1.3 and H1.4 at serine 38 positions. Conclusions: Differences in the level and distribution of H1ph and H3K9me3 were revealed during mitotic phases. ESC-specific phosphorylation sites were identified in a linker histone.
ER -
LEGARTOVA, Sona, Gabriela LOCHMANOVÁ and Eva BARTOVA. The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation. \textit{LIFE-BASEL}. SWITZERLAND: MDPI, 2022, vol.~12, No~6, p.~798-808. ISSN~2075-1729. Available from: https://dx.doi.org/10.3390/life12060798.
|
