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関連する概念動画

Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

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Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
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Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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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...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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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...
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Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
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タンパク質の輸出を促進する膜成分SecDFの構造と機能

Tomoya Tsukazaki1, Hiroyuki Mori, Yuka Echizen

  • 1Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.

Nature
|May 13, 2011
PubMed
まとめ

SecDFは膜チャペロンとして作用し,陽子の運動力を利用して,バクテリアの膜にわたってATP独立のタンパク質転位を推進します. このタンパク質複合体は,タンパク質の輸送と膜タンパク質の生殖を促進します.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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関連する実験動画

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Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
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Published on: December 3, 2010

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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科学分野:

  • バクテリアのタンパク質分泌.
  • 膜タンパク質のバイオゲネシス
  • 輸送の分子メカニズム

背景:

  • タンパク質が細菌の膜を横断するトランスロケーションには,SecYEGトランスロコンとSecAATPaseが含まれています.
  • プロトンの運動力と膜に統合されたSecDF複合体は,このプロセスを強化します.
  • SecDFのトランスロケーションと膜タンパク質バイオゲネシスの正確な機能は,まだ完全に理解されていません.

研究 の 目的:

  • 細菌のタンパク質転位におけるSecDF複合体の構造的および機能的役割を明らかにする.
  • SecDFがタンパク質の輸送を促進するメカニズムを調査する.
  • SecDF媒介による転位に対するプロトン運動力の貢献を決定する.

主な方法:

  • 3.3 Åの解像度でThermus thermophilus SecDFの結晶構造を決定しました.
  • SecDFのペリプラズマドメイン (P1とP4) の高解像度分析を行った.
  • SecDF.の in vitro 転位アッセイと電気生理学的分析を実施しました.

主要な成果:

  • 結晶構造は,擬似対称型トランスメブラン領域 (RND超家族) と周辺プラズマ領域P1およびP4を明らかにした.
  • 周辺プラズマ領域P1は,展開されたタンパク質と結合すると,形状の変化を経験します.
  • SecDFは,陽子の運動力を必要とするATP独立の転位ステップを容易にし,pHと基板の存在に依存する陽子の伝導性を示す.
  • 超膜界面で保存された残留物は,陽子と前タンパク質の移動に不可欠です.

結論:

  • SecDFは,膜に統合されたチャペロンとして機能します.
  • プロトンの運動力は,SecDF.によって媒介されるATP独立のタンパク質転位機構を動かす.
  • SecDFは,陽子伝導と形状の柔軟性を通して,タンパク質の輸送と潜在的に膜タンパク質の生体生成を促進する上で重要な役割を果たしています.