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Starkova TY, Artamonova TO, Ermakova VV, et al. The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells. Acta Naturae. 2019;11(2):82-91doi: 10.32607/20758251-2019-11-2-82-91.
Starkova, T. Y., Artamonova, T. O., Ermakova, V. V., Chikhirzhina, E. V., Khodorkovskii, M. A., & Tomilin, A. N. (2019). The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells. Acta naturae, 11(2), 82-91. https://doi.org/10.32607/20758251-2019-11-2-82-91
Starkova, T Yu, et al. "The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells." Acta naturae vol. 11,2 (2019): 82-91. doi: https://doi.org/10.32607/20758251-2019-11-2-82-91
Starkova TY, Artamonova TO, Ermakova VV, Chikhirzhina EV, Khodorkovskii MA, Tomilin AN. The Profile of Post-translational Modifications of Histone H1 in Chromatin of Mouse Embryonic Stem Cells. Acta Naturae. 2019 Apr-Jun;11(2):82-91. doi: 10.32607/20758251-2019-11-2-82-91. PMID: 31413884; PMCID: PMC6643340.
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Acta Naturae. 2019 Apr-Jun;11(2):82-91. doi: 10.32607/20758251-2019-11-2-82-91.

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

Acta naturae

T Yu Starkova, T O Artamonova, V V Ermakova, E V Chikhirzhina, M A Khodorkovskii, A N Tomilin

Affiliations

  1. Institute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Biology of Stem Cells, Tikhoretsky Ave. 4, St. Petersburg, 194064, Russia.
  2. Peter the Great St.Petersburg Polytechnic University, Politekhnicheskaya Str. 29, St. Petersburg, 195251 , Russia.
  3. Saint Petersburg State University, 13B Universitetskaya Emb., St. Petersburg, 199034, Russia.

PMID: 31413884 PMCID: PMC6643340 DOI: 10.32607/20758251-2019-11-2-82-91

Abstract

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.

Keywords: 2-D electrophoresis; MALDI mass spectrometry; linker histone H1; mouse embryonic stem cells; post-translational modifications

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