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Related Concept Videos

Nucleoid01:24

Nucleoid

The nucleoid represents a structurally and functionally distinct region within prokaryotic cells, where the cell's DNA and associated proteins are housed. Unlike eukaryotic cells, prokaryotes lack a membrane-bound nucleus, and the nucleoid facilitates the organization and accessibility of the genetic material within this constraint. The DNA in most bacteria and archaea exists as a single, circular, double-stranded molecule that is highly compacted through supercoiling and interactions with...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Nuclear Protein Sorting01:34

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Differences in prion strain conformations result from non-native interactions in a nucleus.

Yumiko Ohhashi1, Kazuki Ito, Brandon H Toyama

  • 1Tanaka Research Unit, RIKEN Brain Science Institute, Wako, Saitama, Japan.

Nature Chemical Biology
|January 19, 2010
PubMed
Summary

Protein misfolding into amyloid conformations is temperature-dependent. Non-native interactions in initial protein nuclei drive oligomer formation, influencing prion strain diversity and infectivity.

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Purification of Hsp104, a Protein Disaggregase
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Published on: September 30, 2011

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Last Updated: Jun 17, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

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Published on: January 8, 2015

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

Area of Science:

  • Biochemistry
  • Structural Biology
  • Prion Biology

Background:

  • Aggregation-prone proteins can misfold into various amyloid conformations.
  • Amyloid formation initiates from a transient nucleus, but its formation mechanism and influence on specific conformations remain unclear.

Purpose of the Study:

  • To elucidate the mechanism of initial nucleus formation in amyloidogenesis.
  • To understand how nucleus formation dictates specific amyloid conformations and prion strain phenotypes.

Main Methods:

  • Investigated the prion domain (Sup35NM) of yeast prion Sup35.
  • Utilized mutational and biophysical analyses.
  • Examined temperature-dependent, reversible oligomer formation before fiber assembly.

Main Results:

  • Sup35NM forms temperature-dependent, reversible oligomers prior to fiber formation.
  • Non-native aromatic interactions outside the amyloid core drive oligomerization.
  • Oligomer formation specifically leads to infectious prion strains with limited amyloid cores.

Conclusions:

  • Transient non-native interactions in the initial nucleus are critical for amyloid conformational diversity.
  • These interactions determine the distinct phenotypes of prion strains.