Cargando…

The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells

Linker histone H1 is one of the main chromatin proteins which plays an important role in organizing eukaryotic DNA into a compact structure. There is data indicating that cell type-specific post-translational modifications of H1 modulate chromatin activity. Here, we compared histone H1 variants from...

Descripción completa

Detalles Bibliográficos
Autores principales: Starkova, T. Yu., Artamonova, T. O., Ermakova, V. V., Chikhirzhina, E. V., Khodorkovskii, M. A., Tomilin, A. N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6643340/
https://www.ncbi.nlm.nih.gov/pubmed/31413884
http://dx.doi.org/10.32607/20758251-2019-11-2-82-91
_version_ 1783437108703133696
author Starkova, T. Yu.
Artamonova, T. O.
Ermakova, V. V.
Chikhirzhina, E. V.
Khodorkovskii, M. A.
Tomilin, A. N.
author_facet Starkova, T. Yu.
Artamonova, T. O.
Ermakova, V. V.
Chikhirzhina, E. V.
Khodorkovskii, M. A.
Tomilin, A. N.
author_sort Starkova, T. Yu.
collection PubMed
description Linker histone H1 is one of the main chromatin proteins which plays an important role in organizing eukaryotic DNA into a compact structure. There is data indicating that cell type-specific post-translational modifications of H1 modulate chromatin activity. Here, we compared histone H1 variants from NIH/3T3, mouse embryonic fibroblasts (MEFs), and mouse embryonic stem (ES) cells using matrix-assisted laser desorption/ ionization Fourier transform ion cyclotron resonance mass spectrometry (MALDI-FT-ICR-MS). We found significant differences in the nature and positions of the post-translational modifications (PTMs) of H1.3-H1.5 variants in ES cells compared to differentiated cells. For instance, methylation of K75 in the H1.2-1.4 variants; methylation of K108, K148, K151, K152 K154, K155, K160, K161, K179, and K185 in H1.1, as well as of K168 in H1.2; phosphorylation of S129, T146, T149, S159, S163, and S180 in H1.1, T180 in H1.2, and T155 in H1.3 were identified exclusively in ES cells. The H1.0 and H1.2 variants in ES cells were characterized by an enhanced acetylation and overall reduced expression levels. Most of the acetylation sites of the H1.0 and H1.2 variants from ES cells were located within their C-terminal tails known to be involved in the stabilization of the condensed chromatin. These data may be used for further studies aimed at analyzing the functional role played by the revealed histone H1 PTMs in the self-renewal and differentiation of pluripotent stem cells.
format Online
Article
Text
id pubmed-6643340
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher A.I. Gordeyev
record_format MEDLINE/PubMed
spelling pubmed-66433402019-08-14 The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells Starkova, T. Yu. Artamonova, T. O. Ermakova, V. V. Chikhirzhina, E. V. Khodorkovskii, M. A. Tomilin, A. N. Acta Naturae Research Article Linker histone H1 is one of the main chromatin proteins which plays an important role in organizing eukaryotic DNA into a compact structure. There is data indicating that cell type-specific post-translational modifications of H1 modulate chromatin activity. Here, we compared histone H1 variants from NIH/3T3, mouse embryonic fibroblasts (MEFs), and mouse embryonic stem (ES) cells using matrix-assisted laser desorption/ ionization Fourier transform ion cyclotron resonance mass spectrometry (MALDI-FT-ICR-MS). We found significant differences in the nature and positions of the post-translational modifications (PTMs) of H1.3-H1.5 variants in ES cells compared to differentiated cells. For instance, methylation of K75 in the H1.2-1.4 variants; methylation of K108, K148, K151, K152 K154, K155, K160, K161, K179, and K185 in H1.1, as well as of K168 in H1.2; phosphorylation of S129, T146, T149, S159, S163, and S180 in H1.1, T180 in H1.2, and T155 in H1.3 were identified exclusively in ES cells. The H1.0 and H1.2 variants in ES cells were characterized by an enhanced acetylation and overall reduced expression levels. Most of the acetylation sites of the H1.0 and H1.2 variants from ES cells were located within their C-terminal tails known to be involved in the stabilization of the condensed chromatin. These data may be used for further studies aimed at analyzing the functional role played by the revealed histone H1 PTMs in the self-renewal and differentiation of pluripotent stem cells. A.I. Gordeyev 2019 /pmc/articles/PMC6643340/ /pubmed/31413884 http://dx.doi.org/10.32607/20758251-2019-11-2-82-91 Text en Copyright ® 2019 National Research University Higher School of Economics. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Starkova, T. Yu.
Artamonova, T. O.
Ermakova, V. V.
Chikhirzhina, E. V.
Khodorkovskii, M. A.
Tomilin, A. N.
The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
title The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
title_full The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
title_fullStr The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
title_full_unstemmed The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
title_short The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells
title_sort profile of post-translational modifications of histone h1 in chromatin of mouse embryonic stem cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6643340/
https://www.ncbi.nlm.nih.gov/pubmed/31413884
http://dx.doi.org/10.32607/20758251-2019-11-2-82-91
work_keys_str_mv AT starkovatyu theprofileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT artamonovato theprofileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT ermakovavv theprofileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT chikhirzhinaev theprofileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT khodorkovskiima theprofileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT tomilinan theprofileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT starkovatyu profileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT artamonovato profileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT ermakovavv profileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT chikhirzhinaev profileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT khodorkovskiima profileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells
AT tomilinan profileofposttranslationalmodificationsofhistoneh1inchromatinofmouseembryonicstemcells