関連する実験動画
Updated: May 31, 2026
05:52
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
Get3受容体複合体による尾を固定した膜タンパク質バイオゲネシスの構造的基礎
Susanne Stefer1, Simon Reitz, Fei Wang
1Institute for Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, Goethe University, D-60325 Frankfurt am Main, Germany.
Science (New York, N.Y.)
|July 2, 2011
まとめ
この研究は,尾に固定されたタンパク質が,エンドプラズマの網膜膜にどのように到達するかを明らかにしています. Get3 ATPaseは,Get1/2受容体とともに,この重要な細胞伝達プロセスを促進します.
科学分野:
- 細胞生物学 細胞生物学
- 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:
- テイルアンクルド (TA) タンパク質は,タンパク質の密輸とアポトーシスを含む様々な細胞機能に不可欠です.
- 彼らのC端膜アンカーは,エンドプラズマ網膜 (ER) 膜に翻訳後の挿入のための特定の機械を必要とします.
研究 の 目的:
- ER膜への尾を固定したタンパク質の供給の構造的基礎を解明する.
- Get3 ATPaseとGet1/2受容体との相互作用のメカニズムを理解するために.
主な方法:
- X線結晶学を用いて,Get1とGet2の複合体であるGet3の構造を決定した.
- 構造的発見と機能的相互作用を検証するために生化学実験が行われました.
主要な成果:
- 結晶構造は,Get3がGet1とGet2と複合し,異なる機能状態にあることを明らかにした.
- Get1とGet2は,隣接し,重複するサイトでGet3と結合し,同時結合が可能である.
- 複合形成は,TAタンパク質の挿入に必要なGet3の構造変化を誘導する.
結論:
- Get1/2受容体複合体は,Get3.3と相互作用することで,TAタンパク質の伝達を促進します.
- 構造的および生化学的なデータは,核酸調節されたTAタンパク質がER膜に挿入されるための分子機構を示唆しています.
関連する概念動画
01:45Tail-anchoring of Proteins in the ER Membrane
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
01:26Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
01:29GPI Anchoring of Proteins in the ER Membrane
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
01:20Cotranslational Protein Translocation
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
01:28Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
01:21Structure of Porins
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...