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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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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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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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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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Related Experiment Video

Updated: Nov 25, 2025

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

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HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells.

Haiyang Yu1, Shan Lu2, Kelsey Gasior3,4

  • 1Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla, CA, USA. dcleveland@ucsd.edu haiyang-yu@ucsd.edu.

Science (New York, N.Y.)
|December 18, 2020
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RNA binding protein TDP-43 forms liquid crystal droplets called anisosomes in neurodegenerative diseases. HSP70 chaperones and proteasome activity regulate these structures, preventing toxic aggregation.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Purification of Hsp104, a Protein Disaggregase
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Related Experiment Videos

Last Updated: Nov 25, 2025

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Purification of Hsp104, a Protein Disaggregase
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Area of Science:

  • Neurobiology
  • Biochemistry
  • Molecular Biology

Background:

  • TDP-43 protein aggregation is a hallmark of neurodegenerative diseases.
  • Dysfunctional RNA binding by TDP-43 is linked to its pathological aggregation.

Purpose of the Study:

  • To investigate the biophysical properties of TDP-43 aggregates.
  • To identify factors regulating TDP-43 phase separation and aggregation.

Main Methods:

  • Induction of RNA binding-deficient TDP-43 variants.
  • Formation and characterization of TDP-43 droplets (anisosomes).
  • Mathematical modeling and in vivo experiments.

Main Results:

  • RNA binding-deficient TDP-43 forms liquid spherical shells with liquid cores (anisosomes).
  • Anisosome shells exhibit liquid crystal properties.
  • HSP70 chaperones maintain anisosome liquidity, dependent on ATP.
  • Proteasome inhibition induces anisosomes; reduced ATP causes conversion to aggregates.

Conclusions:

  • Acetylation, HSP70, and proteasome activity are key regulators of TDP-43 phase separation.
  • Anisosomes represent a distinct liquid phase of TDP-43 that can transition to a solid aggregate phase.
  • Understanding these mechanisms may offer therapeutic targets for neurodegenerative diseases.