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Updated: Jun 29, 2025

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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在Fe-S蛋白生物发生过程中的伴侣功能:三个可能的场景

Jaroslaw Marszalek1, Elizabeth A Craig2, Marcin Pitek1

  • 1Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.

Biochimica et biophysica acta. Molecular cell research
|April 4, 2024
PubMed
概括

对于铁硫集群生物生成至关重要的ISC机械,采用了独特的护送系统. 这篇评论探讨了陪伴者.

关键词:
在 Hsc20 中,Hsc20 是 Hsc20 的.在Hsp70中,它是Hsp70的.在Hsp70-基质相互作用周期中.这是一个很好的避难所.在J-域蛋白质中.联合开发计划 (JDP) 的一个部分.

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Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Post-translational Translocation of Proteins to the RER

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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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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.
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