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Updated: Jun 30, 2025

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Published on: January 26, 2018

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两个DOT1酶协同调解有效的无素独立的素H3 lysine 76三甲基化在kinetoplastids中

Victoria S Frisbie1, Hideharu Hashimoto1, Yixuan Xie2,3

  • 1Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA, USA.

Nature communications
|March 20, 2024
PubMed
概括

动态塑DOT1A和DOT1B甲基酸组素H3K76独立于H2B无处不在,与较高的真核生物不同. 关键的残留物和独特的动力学使H3K76的合作性三甲基化成为可能,解释了两个DOT1酶的演化.

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Covalently Linked Protein Regulators

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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