由Aurora B进行的Histone H3 血清10酸化导致HP1与异性染色的解离
Toru Hirota1, Jesse J Lipp, Ban-Hock Toh
1Research Institute of Molecular Pathology, Dr. Bohrgasse 7, A-1030 Vienna, Austria.
Nature
|October 14, 2005
概括
基斯修饰调节了蛋白质与染色素的结合. 通过Aurora B对素H3血清10的酸化,在线粒分裂过程中将异性染色蛋白1 (HP1) 取代,揭示出一种新的甲基/开关机制.
科学领域:
- 表观遗传学和分子生物学
- 染色体生物学 染色体生物学
- 细胞调节 细胞调节 细胞调节
背景情况:
- 基因组经历翻译后的修改,影响染色质结构和蛋白质招募.
- 异染色蛋白1 (HP1) 与三甲基化组素H3氨酸9 (H3K9me3) 结合,由Suv39h进行介导.
- 由Aurora B基因酶发生的基化 (H3S10ph) 发生在线粒分裂过程中,但其功能尚不清楚.
研究的目的:
- 为了研究H3S10ph在线粒分裂过程中的功能作用.
- 阐明基因组修饰调节蛋白质-染色质相互作用的机制.
- 为了识别与自身免疫性疾病相关的抗体所识别的特定的组素修饰模式.
主要方法:
- 使用抗体对抗线性染色体抗原.
- 研究了H3K9me3和H3S10ph之间的相互作用.
- 在抑制H3S10ph的条件下检查HP1与线粒染色体的结合.
- 研究了Suv39h和Aurora B在产生特定基因素标记中的作用.
主要成果:
- 鉴定了一种特定的组素修饰,H3K9me3S10ph,由与自身免疫性疾病相关的抗体识别.
- 证明H3K9me3S10ph的生成是依赖于Suv39h和Aurora B.的.
- 由Aurora B显示,H3S10ph对于HP1与线粒染色体的分离至关重要.
- 观察到抑制H3S10ph可以防止HP1在线粒分裂过程中的解离.
结论:
- 由Aurora B产生的H3S10ph作为"甲基/开关"来取代HP1从线粒异性染色素中取代.
- 这种机制调节细胞分裂期间蛋白质与染色素的结合.
- 这些发现提供了关于在线粒分裂过程中组织蛋白修饰的功能意义以及与自身免疫反应的潜在联系的见解.
相关概念视频
Histone Modification
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 deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Spreading of Chromatin Modifications
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 is an enzyme that can...
Writers
The writer is an enzyme that can...
Histone Variants at the Centromere
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
Heterochromatin
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.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Heterochromatin
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.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Histone Modification
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 deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...


