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suck abstract from ncbi


10.1126/science.aai7776

http://scihub22266oqcxt.onion/10.1126/science.aai7776
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C5460984!5460984 !28082594
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suck abstract from ncbi


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pmid28082594
      Science 2017 ; 355 (6321 ): 198-201
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  • A bacterial global regulator forms a prion #MMPMID28082594
  • Yuan AH ; Hochschild A
  • Science 2017[Jan]; 355 (6321 ): 198-201 PMID28082594 show ga
  • Prions are self-propagating protein aggregates that act as protein-based elements of inheritance in fungi. Although prevalent in eukaryotes, prions have not been identified in bacteria. Here we found that a bacterial protein, transcription terminator Rho of Clostridium botulinum (Cb-Rho), could form a prion. We identified a candidate prion-forming domain (cPrD) in Cb-Rho and showed that it conferred amyloidogenicity on Cb-Rho and could functionally replace the PrD of a yeast prion-forming protein. Furthermore, its cPrD enabled Cb-Rho to access alternative conformations in Escherichia coli-a soluble form that terminated transcription efficiently and an aggregated, self-propagating prion form that was functionally compromised. The prion form caused genome-wide changes in the transcriptome. Thus, Cb-Rho functions as a protein-based element of inheritance in bacteria, suggesting that the emergence of prions predates the evolutionary split between eukaryotes and bacteria.
  • |Amino Acid Sequence [MESH]
  • |Amyloid/chemistry/*metabolism [MESH]
  • |Bacterial Proteins/chemistry/genetics/*metabolism [MESH]
  • |Clostridium botulinum/*metabolism [MESH]
  • |Escherichia coli/metabolism [MESH]
  • |Evolution, Molecular [MESH]
  • |Prions/*metabolism [MESH]
  • |Protein Domains [MESH]
  • |Rho Factor/chemistry/genetics/*metabolism [MESH]


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