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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

4.4K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.4K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

4.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
4.1K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.1K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

3.3K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
3.3K

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Updated: Sep 9, 2025

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
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ダイナミックTOM-TIM23超複合体は,ミトコンドリアタンパク質の転位と分類を指揮する.

Yuqi Yang1, Shanshan Wang1, Guopeng Wang2

  • 1State Key Laboratory of Membrane Biology, School of Life Sciences, Peking University, Beijing, China.

Nature structural & molecular biology
|August 28, 2025
PubMed
まとめ

研究者はミトコンドリアのTOM-TIM23超複合体を視覚化して タンパク質がミトコンドリアの膜にどのように配列されているかを明らかにしました これは,ミトコンドリアのタンパク質の輸入と分類のメカニズムに関する新しい洞察を提供します.

さらに関連する動画

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components

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Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
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Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

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関連する実験動画

Last Updated: Sep 9, 2025

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
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科学分野:

  • ミトコンドリア生物学
  • 分子生物学と構造生物学

背景:

  • ミトコンドリアへのタンパク質の輸入は 細胞の機能に不可欠です
  • 外膜のミトコンドリアトランスロカゼ (TOM) と内膜のトランスロカゼ23 (TIM23) コンプレックスは,ミトコンドリア膜のタンパク質トランスロケーションを媒介する.
  • 結合されたTOM-TIM23経路内の基板認識と分類の正確なメカニズムは完全に理解されていません.

研究 の 目的:

  • TOM-TIM23経路におけるタンパク質認識と分類の基礎となる構造的メカニズムを解明する.
  • トランスロケーションするポリペプチドとTOM-TIM23超複合体の間のダイナミックな相互作用を視覚化します.

主な方法:

  • クリオ電子顕微鏡 (cryo-EM) を用いて,転位ポリペプチド基板によるTOM-TIM23超複合体の構造を決定した.
  • 構造分析は,ポリペプチドの構造と,TOMとTIM23複合体のサブユニットとの相互作用に焦点を当てた.

主要な成果:

  • この研究では,TOM複合体内のポリペプチド基板の複数の構成が,TOM40チャネルの水性残留によって安定させられた.
  • TIM23複合転位経路は,TIM17およびMgr2サブユニットを含み,基板の水害性によって調節される水害性収縮を特徴としています.
  • 基板の水嫌性は,Mgr2- Tim17結合を動的に調節し,ミトコンドリアマトリックスまたは膜へのタンパク質の分類を制御する.

結論:

  • この発見は,TOM-TIM23超複合体内の洗練された転位メカニズムを示しています.
  • このメカニズムは,多様なミトコンドリアのタンパク質の効率的で規制された輸入を保証します.
  • 構造的な洞察は,ミトコンドリアのタンパク質輸入障害を理解するための基礎を提供します.