[PHI+], a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104

Colin G. Crist, Toru Nakayashiki, Hiroshi Kurahashi, Yoshikazu Nakamura

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

Abstract

Background: The [PSI+] element of the budding yeast is an aggregated form of the translation release factor Sup35 that is propagated and transmitted cytoplasmically in a manner analogous to that of mammalian prions. The N-terminal of Sup35, necessary for [PSI+], contains oligopeptide repeats and multiple G1n/Asn residues. Results: We replaced the Gln/Asn-rich prion repeats of Sup35 with non-Gln/Asn repeats from heterologous yeast strains. These non-Gln/Asn repeat Sup35s propagated a novel [PSI+] variant, [PHI+], that appeared de novo 103 times more frequent than [PSI+]. [PHI+] was stably inherited in a non-Mendelian fashion, but not eliminated upon the inactivation of Hsp104, unlike known [PSI+] elements. In vitro, non-Gln/Asn repeat domains formed amyloid fibres that were shorter and grew more slowly than did Gln/Asn-rich prion domains, while [PHI+] aggregates were smaller than [PSI+] aggregates in vivo. Conclusions: These findings suggest the existence of an alternative, Hsp104-independent pathway to replicate non-Gln/Asn variant Sup35 prion seeds.

Original languageEnglish
Pages (from-to)603-618
Number of pages16
JournalGenes to Cells
Volume8
Issue number7
DOIs
Publication statusPublished - 2003 Jul 1

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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