Prion propagation can occur in a prokaryote and requires the ClpB chaperone

Abstract
Article and author information
Metrics

Abstract

Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals, the PrP protein can form a prion that causes the fatal transmissible spongiform encephalopathies. Prions have also been uncovered in fungi, where they act as heritable, protein-based genetic elements. We previously showed that the yeast prion protein Sup35 can access the prion conformation in Escherichia coli. Here we demonstrate that E. coli can propagate the Sup35 prion under conditions that do not permit its de novo formation. Furthermore, we show that propagation requires the disaggregase activity of the ClpB chaperone. Prion propagation in yeast requires Hsp104 (a ClpB ortholog), and prior studies have come to conflicting conclusions about ClpB's ability to participate in this process. Our demonstration of ClpB-dependent prion propagation in E. coli suggests that the cytoplasmic milieu in general and a molecular machine in particular are poised to support protein-based heredity in the bacterial domain of life.

Article and author information

Author details

Andy H Yuan

Harvard Medical School, Boston, United States

Competing interests
The authors declare that no competing interests exist.
Sean J Garrity

Harvard Medical School, Boston, United States

Competing interests
The authors declare that no competing interests exist.
Entela Nako

Harvard Medical School, Boston, United States

Competing interests
The authors declare that no competing interests exist.
Ann Hochschild

Harvard Medical School, Boston, United States

For correspondence
ahochschild@hms.harvard.edu

Competing interests
The authors declare that no competing interests exist.

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.