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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
The...
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Molecular Chaperones and Protein Folding03:00

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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 Folding Quality Check in the RER01:29

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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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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14.

Nikoletta Murvai1,2, Lajos Kalmar1,3, Beata Szabo1

  • 1Research Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.

International Journal of Molecular Sciences
|July 2, 2021
PubMed
Summary
This summary is machine-generated.

Plant intrinsically disordered proteins, like dehydrins, protect against stress. The study shows all conserved regions of ERD14 are crucial for its protective function, working together for cellular survival.

Keywords:
CD spectroscopyLEA proteindehydrinearly response to dehydrationheat stressintrinsic structural disorderplant chaperonestructure-function relationship

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Area of Science:

  • Plant biology
  • Molecular biology
  • Biochemistry

Background:

  • Intrinsically disordered proteins (IDPs) function as chaperones, aiding plant survival under abiotic stress.
  • Dehydrins are a major class of IDPs, upregulated during drought, heat, and osmotic stress.
  • Conserved sequence motifs define dehydrins, but their specific roles in function are unclear.

Purpose of the Study:

  • To investigate the functional relevance of conserved segments within the intrinsically disordered stress protein (IDSP) Early Response to Dehydration 14 (ERD14).
  • To determine how individual conserved regions contribute to the protective capabilities of ERD14.

Main Methods:

  • Analysis of conserved sequence motifs in ERD14, an intrinsically disordered stress protein.
  • Functional assessment of ERD14's protective role in plant cells under stress conditions.
  • Investigating the contribution of specific conserved segments to ERD14's partner binding and overall function.

Main Results:

  • Both partner-binding and non-partner-binding conserved segments are essential for ERD14's protective function.
  • Cellular protection mediated by ERD14 arises from the coordinated interaction of its distinct regions.
  • The study highlights the importance of the interplay between different regions for protein efficacy.

Conclusions:

  • All conserved segments of ERD14 are indispensable for its role as a protective chaperone.
  • The balanced interplay of conserved regions is critical for the functional efficacy of intrinsically disordered stress proteins.
  • This research provides insights into the structure-function relationship of dehydrins and their role in plant stress tolerance.