関連する実験動画

Updated: Jan 5, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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Hsp40チャペロンの顧客認識と活動の構造的基礎

Yajun Jiang1, Paolo Rossi1, Charalampos G Kalodimos2

  • 1Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.

Science (New York, N.Y.)
|October 12, 2019
PubMed
まとめ

熱ショックタンパク質40 (Hsp40) チャペロンは,展開されたクライアントタンパク質に動的に結合し,その折り畳み特性を変化させます. Hsp70とHsp40の結合は,このクライアント相互作用を制御し,タンパク質の折り畳みを制御します.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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Intracellular Refolding Assay07:18

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Molecular Chaperones and Protein Folding03:00

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Energy to Drive Translocation

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...
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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