関連する実験動画
Updated: Jun 13, 2026
11:36
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
ヘテロテトラメリックSAGAヒストンH2Bデウビキキチナゼモジュールの組立と活性化の構造的基礎
Alwin Köhler1, Erik Zimmerman, Maren Schneider
1Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. alwin.koehler@mfpl.ac.at
Cell
|May 4, 2010
まとめ
SAGAのデウビキチン化酵素 (DUB) モジュールです.
科学分野:
- バイオケミストリー バイオケミストリー
- 分子生物学は分子生物学である.
- 構造生物学 構造生物学とは
背景:
- デユビキチン化酵素 (DUB) は,細胞過程の重要な調節因子である.
- 異なる細胞環境におけるDUB活動を制御する特定のメカニズムは,完全に解明されていません.
- SAGA複合体は,酵母デウビキチン酵素 Ubp8.8 を誘発し,活性化させます.
研究 の 目的:
- 完全なSAGA DUBモジュールの結晶構造を決定するために.
- Ubp8の非基板パートナーによるアクティベーションと規制の構造的基盤を明らかにする.
- ヒストンH2Bデウビキチン化におけるSgf11とSgf73の役割を理解する.
主な方法:
- SAGA DUBモジュールの構造を得るためのX線結晶学.
- DUBモジュールのコンポーネントの機能を分析するための生化学分析.
- 構造ベースの機能分析.
主要な成果:
- 結晶構造は,Sgf73.3で結びついているSAGA DUBモジュールの2葉構造を明らかにしています.
- Sus1とSgf11は,別々の葉でUbp8と相互作用し",組み立て葉"と"触媒葉"を形成する.
- Sgf11の亜鉛指ドメインは,Ubp8の活性部位の近くに位置し,Sgf73は支架として機能する.
結論:
- Sgf11とSgf73は,Ubp8.8のアロステリック活性化に不可欠な役割を果たしています.
- SAGA DUBモジュール構造は,非基板タンパク質によってDUBがどのように調節されるかについての洞察を提供します.
- この研究は,デウビキチン化酵素をそのパートナーによってアロステリック調節するメカニズムを明らかにしています.
関連する概念動画
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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,...
02:32Histone 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...
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...