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相关概念视频

Histone Modification02:32

Histone Modification

16.9K
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.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.9K
Histone Modification02:32

Histone Modification

4.8K
4.8K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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.
Writers
The writer...
9.9K
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

2.3K
Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
2.3K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.9K
Nucleosome Remodeling02:54

Nucleosome Remodeling

11.5K
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.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
11.5K

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相关实验视频

Updated: Mar 15, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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在SIRT2中逆转4-Oxononanoyl Lysine对Histon的改变

Jing Jin1, Bin He2, Xiaoyu Zhang3

  • 1School of Biomedical Science, University of Hong Kong , Hong Kong, China.

Journal of the American Chemical Society
|September 10, 2016
PubMed
概括

哺乳动物的SIRT2可以去除新发现的组织蛋白修饰,即素4-氧纳基化 (4-ON基化),这对于理解氧化应激反应至关重要.

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科学领域:

  • 生物化学
  • 分子生物学
  • 细胞生物学

背景情况:

  • 翻译后的修改对于蛋白质功能和生物过程至关重要.
  • 氨酸4-氧纳基化 (4-ONylation) 是最近发现的核素PTM,在氧化应激过程中抑制核素组合.
  • 负责逆转4-ONylation的酶仍然未被确定,限制了对其细胞作用的研究.

研究的目的:

  • 识别能够从组织蛋白中去除4-ONyl修饰的细胞酶.
  • 阐明4-ONylation逆转的机制.
  • 了解SIRT2在氧化应激和4-ONylation中的作用.

主要方法:

  • 在实验室测试4-ONylated蛋白质上的SIRT2活性.
  • 用4-ONyl复合体确定SIRT2的晶体结构.
  • 细胞实验验证SIRT2在4-ONylation去除中的作用.

主要成果:

  • 哺乳动物SIRT2被确定为一种酶,可以从活细胞中的基因组和其他蛋白质中去除4-ONyl修饰.
  • 晶体结构揭示了Phe119与4-ONyl组的氧之间的关键单对π相互作用.
  • 这项研究提供了第一个反转4-ONyl lysine修饰机制的证据.

结论:

  • 在逆转 lysine 4-oxononanoylation 中,SIRT2 的作用至关重要.
  • 这些发现提供了SIRT2在氧化应激反应途径中的功能.
  • 这项工作有助于进一步研究4-ONylation的生物学意义.