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Related Concept Videos

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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. 
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Amyloid Fibrils03:03

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Yeast cell adhesion molecules have functional amyloid-forming sequences.

Caleen B Ramsook1, Cho Tan, Melissa C Garcia

  • 1Department of Biology, Brooklyn College, Brooklyn, NY 11210, USA.

Eukaryotic Cell
|December 30, 2009
PubMed
Summary

Yeast cell adhesion proteins, including adhesins from Candida albicans and Saccharomyces cerevisiae, possess amyloid-forming sequences. These amyloids are crucial for cellular aggregation and flocculation, impacting yeast cell interactions.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Amyloid-forming sequences were identified in Candida albicans Als proteins.
  • This discovery prompted an investigation into similar sequences in other yeast adhesins.

Purpose of the Study:

  • To identify and characterize amyloid-forming sequences in adhesins from Candida albicans and Saccharomyces cerevisiae.
  • To determine the role of these amyloid structures in yeast cell aggregation and adhesion.

Main Methods:

  • Utilized the beta-aggregation predictor TANGO to identify aggregation-prone sequences.
  • Synthesized peptides and expressed protein fragments for in vitro amyloid formation assays (Congo red absorbance, thioflavin T fluorescence, fiber morphology).
  • Assessed in vivo amyloid formation using microscopy and thioflavin T binding on yeast cells.

Main Results:

  • Amyloid-forming sequences, rich in Ile, Thr, and Val, were found in most yeast adhesins.
  • Peptides and protein fragments rapidly formed insoluble amyloids in vitro.
  • In vivo, yeast cells expressing adhesins exhibited amyloid properties, with increased aggregation and dye binding.
  • Amyloid dyes inhibited cell aggregation and flocculation.

Conclusions:

  • Amyloid formation is an intrinsic property of numerous yeast cell adhesion proteins.
  • Amyloid structures play a significant role in mediating cellular aggregation and flocculation in yeast.