Skip to main content

The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe

Sideri, Theodora, Yashiroda, Yoko, Ellis, David, Rodriguez-Lopez, Maria, Yoshida, Minoru, Tuite, Mick F., Bahler, Jurg (2017) The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe. Microbial Cell, 4 (1). pp. 16-28. ISSN 2311-2638. (doi:10.15698/mic2017.01.552) (KAR id:60563)

PDF Publisher pdf
Language: English


Download this file
(PDF/3MB)
[thumbnail of 2016A-Sideri_Microbial-Cell.pdf]
Preview
Request a format suitable for use with assistive technology e.g. a screenreader
PDF Author's Accepted Manuscript
Language: English

Restricted to Repository staff only
Contact us about this Publication
[thumbnail of Sideri et al 2017 Microbial Cell - Author Manuscript.pdf]
Official URL:
http://dx.doi.org/10.15698/mic2017.01.552

Abstract

Prions are protein-based infectious entities associated with fatal brain diseases in animals, but also modify a range of host-cell phenotypes in the budding yeast, Saccharomyces cerevisiae. Many questions remain about the evolution and biology of prions. Although several functionally distinct prion-forming proteins exist in S. cerevisiae, [HET-s] of Podospora anserina is the only other known fungal prion. Here we investigated prion-like, protein-based epigenetic transmission in the fission yeast Schizosaccharomyces pombe. We show that S. pombe cells can support the formation and maintenance of the prion form of the S. cerevisiae Sup35 translation factor [PSI+], and that the formation and propagation of these Sup35 aggregates is inhibited by guanidine hydrochloride, indicating commonalities in prion propagation machineries in these evolutionary diverged yeasts. A proteome-wide screen identified the Ctr4 copper transporter subunit as a putative prion with a predicted prion-like domain. Overexpression of the ctr4 gene resulted in large Ctr4 protein aggregates that were both detergent and proteinase-K resistant. Cells carrying such [CTR+] aggregates showed increased sensitivity to oxidative stress, and this phenotype could be transmitted to aggregate-free [ctr–] cells by transformation with [CTR+] cell extracts. Moreover, this [CTR+] phenotype was inherited in a non-Mendelian manner following mating with naïve [ctr–] cells, but intriguingly the [CTR+] phenotype was not eliminated by guanidine-hydrochloride treatment. Thus, Ctr4 exhibits multiple features diagnostic of other fungal prions and is the first example of a prion in fission yeast. These findings suggest that transmissible protein-based determinants of traits may be more widespread among fungi.

Item Type: Article
DOI/Identification number: 10.15698/mic2017.01.552
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 27 Feb 2017 13:49 UTC
Last Modified: 04 Mar 2024 17:41 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/60563 (The current URI for this page, for reference purposes)

University of Kent Author Information

  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.