Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28082594
.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Science
2017 ; 355
(6321
): 198-201
Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
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.