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[PHI+], a novel Sup35‐prion variant propagated with non‐Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104
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 mul...
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Published in: | Genes to cells : devoted to molecular & cellular mechanisms 2003-07, Vol.8 (7), p.603-618 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 Gln/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. |
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ISSN: | 1356-9597 1365-2443 |
DOI: | 10.1046/j.1365-2443.2003.00661.x |