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Protein Misfolding Cyclic Amplification of Prions
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A bacterial global regulator forms a prion.

Andy H Yuan1, Ann Hochschild2

  • 1Department of Microbiology and Immunobiology, Harvard Medical School, 4 Blackfan Circle, Boston, MA 02115, USA.

Science (New York, N.Y.)
|January 14, 2017
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Summary
This summary is machine-generated.

Bacteria can form prions, which are self-propagating protein aggregates. Researchers discovered a bacterial protein, Rho, that can form a prion, suggesting prions existed before eukaryotes and bacteria diverged.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Prions are known eukaryotic protein-based inheritance elements, characterized by self-propagating aggregates.
  • Prions have not been previously identified in bacterial systems.
  • Understanding prion origins and distribution is crucial for evolutionary biology.

Purpose of the Study:

  • To investigate the potential for prion formation in bacterial proteins.
  • To identify and characterize the prion-forming capabilities of bacterial Rho transcription terminator (Cb-Rho).
  • To explore the evolutionary implications of bacterial prion discovery.

Main Methods:

  • Identification of a candidate prion-forming domain (cPrD) within Cb-Rho.
  • Functional assays in yeast to test the cPrD's ability to replace a known prion domain (PrD).
  • Expression and characterization of Cb-Rho conformations in Escherichia coli, including soluble and aggregated prion forms.
  • Transcriptomic analysis to assess the impact of the Cb-Rho prion form on genome-wide gene expression.

Main Results:

  • The bacterial protein Cb-Rho was identified as capable of forming a prion.
  • A specific cPrD in Cb-Rho conferred amyloidogenicity and could functionally substitute for yeast PrDs.
  • Cb-Rho adopted alternative conformations in E. coli: a soluble, transcriptionally active form and a self-propagating, functionally compromised prion form.
  • The prion form of Cb-Rho induced significant genome-wide transcriptome changes.

Conclusions:

  • Bacterial proteins, like Cb-Rho, can function as protein-based inheritance elements.
  • The discovery of bacterial prions suggests their emergence predates the evolutionary divergence of eukaryotes and bacteria.
  • This finding expands the known scope of prion biology and its evolutionary history.