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Spatial Separation of Molecular Conformers and Clusters
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Molecular basis for diversification of yeast prion strain conformation

Yumiko Ohhashi1,2, Yoshiki Yamaguchi3, Hiroshi Kurahashi1

  • 1Laboratory for Protein Conformation Diseases, RIKEN Brain Science Institute, Wako, 351-0198 Saitama, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|February 23, 2018
PubMed

Insights

Altered protein structures in natively disordered monomers can lead to diverse amyloid conformations. This conformational diversity influences cellular phenotypes and disease outcomes, revealing a new mechanism for protein aggregation.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Amyloid fibers, rich in β-sheets, are protein aggregates linked to cellular dysfunction and diseases.
  • Different amyloid conformations result in varied physiological consequences, including cellular toxicity.
  • The origins of amyloid conformational diversity remain largely unknown.

Purpose of the Study:

  • To investigate the origins of diverse amyloid conformations.
  • To explore the role of conformational equilibrium in natively disordered proteins.
  • To understand how altered monomer structures influence amyloid phenotypes.

Main Methods:

  • Comprehensive high-resolution structural analysis of Sup35NM, a yeast prion protein fragment.
  • Utilized genetic mutations and solvent conditions to alter monomeric structures.
  • Investigated the impact on amyloid conformation, chaperone interactions, and prion phenotypes.

Main Results:

  • Monomeric Sup35NM possesses latent local compact structures within its disordered conformation.
  • Relaxation of these microstructures induced distinct amyloid conformations.
  • Altered amyloid structures affected chaperone-mediated fiber fragmentation and prion strain phenotypes.

Conclusions:

  • Dynamic conformational fluctuations in natively disordered monomers are a key factor in amyloid diversity.
  • This provides a post-translational mechanism for diversifying aggregate structures and cellular phenotypes.
  • Understanding this mechanism is crucial for deciphering amyloid-related diseases.
Keywords:
aggregateamyloidprotein dynamicsprotein misfoldingyeast prion

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