Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions
- PMID: 28639249
- DOI: 10.1007/5584_2017_58
Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions
Abstract
The organisation of chromatin is first discussed to conclude that nucleosomes play both structural and transcription-regulatory roles. The presence of nucleosomes makes difficult the access of transcriptional factors to their target sequences and the action of RNA polymerases. The histone post-translational modifications and nucleosome remodelling are first discussed, from a historical point of view, as mechanisms to remove the obstacles imposed by chromatin structure to transcription. Instead of reviewing the state of the art of the whole field, this review is centred on some open questions. First, some "non-classical" histone modifications, such as short-chain acylations other than acetylation, are considered to conclude that their relationship with the concentration of metabolic intermediaries might make of them a sensor of the physiological state of the cells. Then attention is paid to the interest of studying chromatin organisation and epigenetic marks at a single nucleosome level as a complement to genome-wide approaches. Finally, as a consequence of the above questions, the review focuses on the presence of multiple histone post-translational modifications on a single nucleosome. The methods to detect them and their meaning, with special emphasis on bivalent marks, are discussed.
Keywords: Chromatin; Epigenetics; Histone post-translational modifications; Metabolism and histone modifications; Nucleosome.
Similar articles
-
"Direct" and "Indirect" Effects of Histone Modifications: Modulation of Sterical Bulk as a Novel Source of Functionality.Bioessays. 2020 Jan;42(1):e1900136. doi: 10.1002/bies.201900136. Epub 2019 Dec 5. Bioessays. 2020. PMID: 31805213 Review.
-
Histone modification: cause or cog?Trends Genet. 2011 Oct;27(10):389-96. doi: 10.1016/j.tig.2011.06.006. Epub 2011 Jul 20. Trends Genet. 2011. PMID: 21764166
-
Histone structure and nucleosome stability.Expert Rev Proteomics. 2005 Oct;2(5):719-29. doi: 10.1586/14789450.2.5.719. Expert Rev Proteomics. 2005. PMID: 16209651 Free PMC article. Review.
-
Directed Nucleosome Sliding during the Formation of the Simian Virus 40 Particle Exposes DNA Sequences Required for Early Transcription.J Virol. 2019 Feb 5;93(4):e01678-18. doi: 10.1128/JVI.01678-18. Print 2019 Feb 15. J Virol. 2019. PMID: 30518654 Free PMC article.
-
Nucleosome Clutches are Regulated by Chromatin Internal Parameters.J Mol Biol. 2021 Mar 19;433(6):166701. doi: 10.1016/j.jmb.2020.11.001. Epub 2020 Nov 9. J Mol Biol. 2021. PMID: 33181171 Free PMC article.
Cited by
-
Integrated Genomic and Proteomic Analyses Reveal Novel Mechanisms of the Methyltransferase SETD2 in Renal Cell Carcinoma Development.Mol Cell Proteomics. 2019 Mar;18(3):437-447. doi: 10.1074/mcp.RA118.000957. Epub 2018 Nov 28. Mol Cell Proteomics. 2019. PMID: 30487242 Free PMC article.
-
The Jumonji Domain-Containing Histone Demethylase Homolog 1D/lysine Demethylase 7A (JHDM1D/KDM7A) Is an Epigenetic Activator of RHOJ Transcription in Breast Cancer Cells.Front Cell Dev Biol. 2021 Jun 23;9:664375. doi: 10.3389/fcell.2021.664375. eCollection 2021. Front Cell Dev Biol. 2021. PMID: 34249916 Free PMC article.
-
ZNF518B gene up-regulation promotes dissemination of tumour cells and is governed by epigenetic mechanisms in colorectal cancer.Sci Rep. 2019 Jun 27;9(1):9339. doi: 10.1038/s41598-019-45411-9. Sci Rep. 2019. PMID: 31249328 Free PMC article.
-
Identifying the culprits in neurological autoimmune diseases.J Transl Autoimmun. 2019 Sep 6;2:100015. doi: 10.1016/j.jtauto.2019.100015. eCollection 2019 Dec. J Transl Autoimmun. 2019. PMID: 32743503 Free PMC article. Review.
-
Top-Down Proteomics of Medicinal Cannabis.Proteomes. 2019 Sep 24;7(4):33. doi: 10.3390/proteomes7040033. Proteomes. 2019. PMID: 31554318 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources