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Updated: Sep 13, 2025

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在SWI/SNF基因组沉积中,基因组变异H2A.B的非染色体调节功能

Xuanzhao Jiang1, Jiayu Wen1,2, Mary L Nelson3

  • 1The John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia.

Science advances
|July 25, 2025
PubMed
概括

基斯顿变异H2A.B在霍奇金淋巴瘤中起作用. 它的翻译后修饰 (PTMs),包括化和甲基化,调节其基因组相互作用和转录开始部位活动.

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
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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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