ユカリオットMCM複合体の構造 3.8 Å
Ningning Li1, Yuanliang Zhai2, Yixiao Zhang1
1Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Nature
|July 30, 2015
まとめ
この研究は,酵母におけるミニ染色体維持 (MCM2-7) ヘリケーズ二重ヘクサマーの近原子構造を明らかにした. 複製の起源の活性化時に DNAが溶けるための新しいメカニズムを示唆しています
科学分野:
- 分子生物学
- 構造生物学
- 生物化学
背景:
- DNA複製はユーカリ生物の基本的なプロセスで,複数のメカニズムによって厳密に規制されています.
- ミニ染色体維持 (MCM2-7) ヘリケーゼ複合体は,原点でのDNA複製の開始に不可欠である.
- G1フェーズにおけるMCM2-7ダブルヘクサマーの組み立ては,重要な規制段階です.
研究 の 目的:
- 酵母G1染色体からのMCM2-7二重六合体の近原子構造を決定する.
- 不活性なダブルヘクサマー形成の構造的基礎を解明する.
- DNAの溶解と複製の始まりの仕組みを理解する
主な方法:
- クリオ電子顕微鏡 (cryo-EM) を用いてMCM2-7のダブルヘクサマーを可視化した.
- 酵母G1染色体からMCM2-7ダブルヘクサマーを浄化した.
- 構造分析は,サブユニットとDNAの相互作用の配置に焦点を当てました.
主要な成果:
- G1状態の酵母MCM2-7のダブルヘクサマーの近原子構造が得られた.
- 構造は2つの単一のヘクサマーで 傾斜と歪んだ形状で配置されています
- 互換ドメインとβヘアピンによって形成された,狭い通路を持つ歪んだ中央チャネルが,緊密に結合する二重DNAを観察した.
- ゲート形成サブユニット (MCM2とMCM5) はDNA結合チャネルを横切っている.
結論:
- 単一のヘクサマーの独特の歪みと傾きの配置は,複製の起源でDNAが溶けるメカニズムを示唆しています.
- 干渉DNAの構造的変形は,起源の融解のために必要である可能性が高い.
- 発見は,真核生物におけるDNA複製の開始の調節に関する洞察を提供します.
関連する概念動画
The Supercomplexes in the Crista Membrane
3.2K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
3.2K
Electron Transport Chain: Complex III and IV
9.8K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
9.8K
Assembly of Complex Microtubule Structures
2.8K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
2.8K
Protein Complex Assembly
17.1K
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...
17.1K
Microtubule Formation
8.2K
Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation...
8.2K
Protein Complexes with Interchangeable Parts
2.2K
2.2K


