関連する実験動画
Updated: Jun 27, 2026
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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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COMPASSによって媒介されるH2Bモノウビキチン化とH3メチル化間のヒストンの交差
Jung-Shin Lee1, Abhijit Shukla, Jessica Schneider
1Stowers Institute for Medical Research, 1000 East 50(th) Street, Kansas City, MO 64110, USA.
Cell
|December 18, 2007
まとめ
ヒストンH2Bモノウビキチネーションは,Cps35.5経由でCOMPASS複合体の結合を制御する. この重要なサブユニットは,H2Bの改変をH3K4とH3K79のメチル化と結びつけ,重要なヒストンのクロストラックメカニズムを明らかにします.
科学分野:
- エピジェネティクス エピジェネティクス
- 分子生物学は分子生物学である.
- イースト遺伝学 イースト遺伝学
背景:
- COMPASSは,H3K4メチル化に関与する酵母ヒストンメチルトランスフェラーゼ複合体です.
- ヒストンH2BのモノビキチネーションはH3K4とH3K79のメチル化に不可欠ですが,そのメカニズムは不明です.
- Cps35は,COMPASS複合体の唯一の必須サブユニットです.
研究 の 目的:
- ヒストンH2Bモノウビキチン化とCOMPASS媒介によるH3メチル化とを結びつける分子機構を解明する.
- ヒストンのクロストークを媒介するCps35の役割を調査する.
主な方法:
- COMPASS複合体の生化学的浄化について.
- 野生型および変異性酵母菌株 (例えば,Deltarad6) のCOMPASS活性に関する分析.
- Cps35.5のクロマチン関連研究
主要な成果:
- ヒストンH2Bモノウビキチネーションは,COMPASS複合体へのCps35結合を調節する.
- Cps35は,COMPASSの in vivo触媒活性に不可欠である.
- 外因的なCps35は,H2Bモノウビキチネーションが欠けているCOMPASSにメチル化活動を復元することができます.
- Cps35の染色体関連はH2BK123のモノウビキチネーションに依存するが,Set1.1はそうではない.
- Cps35はH3K79トリメチル化にも必要である.
結論:
- Cps35は,H2Bモノウビキチネーション信号をH3メチル化に変換する重要な媒介者として作用します.
- この研究は,H3K4およびH3K79メチル化におけるH2B変異とCOMPASS機能の間の分子関連性を明らかにしています.
- この発見は,ヒストンの改変を制御する複雑なクロストークメカニズムについての洞察を提供します.
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関連する概念動画
02:10The Nucleosome Core Particle
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
02:32Histone 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,...
02:25Spreading 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...
02:30Histone 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...
02:32Histone 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,...
01:12The Nucleosome Core Particle
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...