{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T13:04:17Z","timestamp":1771333457618,"version":"3.50.1"},"reference-count":98,"publisher":"Oxford University Press (OUP)","issue":"1","funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000062","name":"National Institute of Diabetes and Digestive and Kidney Diseases","doi-asserted-by":"publisher","award":["DK024950"],"award-info":[{"award-number":["DK024950"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,5,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>[URE3] is a prion of the nitrogen catabolism controller, Ure2p, and [PSI+] is a prion of the translation termination factor Sup35p in S. cerevisiae. Btn2p cures [URE3] by sequestration of Ure2p amyloid filaments. Cur1p, paralogous to Btn2p, also cures [URE3], but by a different (unknown) mechanism. We find that an array of mutations impairing proteasome assembly or MG132 inhibition of proteasome activity result in loss of [URE3]. In proportion to their prion\u2014curing effects, each mutation affecting proteasomes elevates the cellular concentration of the anti-prion proteins Btn2 and Cur1. Of &amp;gt;4,600 proteins detected by SILAC, Btn2p was easily the most overexpressed in a pre9\u0394 (\u03b13 core subunit) strain. Indeed, deletion of BTN2 and CUR1 prevents the prion\u2014curing effects of proteasome impairment. Surprisingly, the 15 most unstable yeast proteins are not increased in pre9\u0394 cells suggesting altered proteasome specificity rather than simple inactivation. Hsp42, a chaperone that cooperates with Btn2 and Cur1 in curing [URE3], is also necessary for the curing produced by proteasome defects, although Hsp42p levels are not substantially altered by a proteasome defect. We find that pre9\u0394 and proteasome chaperone mutants that most efficiently lose [URE3], do not destabilize [PSI+] or alter cellular levels of Sup35p. A tof2 mutation or deletion likewise destabilizes [URE3], and elevates Btn2p, suggesting that Tof2p deficiency inactivates proteasomes. We suggest that when proteasomes are saturated with denatured\/misfolded proteins, their reduced degradation of Btn2p and Cur1p automatically upregulates these aggregate-handling systems to assist in the clean-up.<\/jats:p>","DOI":"10.1093\/genetics\/iyab037","type":"journal-article","created":{"date-parts":[[2021,3,20]],"date-time":"2021-03-20T10:35:10Z","timestamp":1616236510000},"source":"Crossref","is-referenced-by-count":8,"title":["Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in <i>Saccharomyces cerevisiae<\/i>"],"prefix":"10.1093","volume":"218","author":[{"given":"Herman K","family":"Edskes","sequence":"first","affiliation":[{"name":"Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emily E","family":"Stroobant","sequence":"additional","affiliation":[{"name":"Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Morgan P","family":"DeWilde","sequence":"additional","affiliation":[{"name":"Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Evgeny E","family":"Bezsonov","sequence":"additional","affiliation":[{"name":"Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reed B","family":"Wickner","sequence":"additional","affiliation":[{"name":"Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2021,4,1]]},"reference":[{"key":"2021070806054974900_iyab037-B1","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1080\/19336896.2015.1022022","article-title":"The ribosome-associated complex antagonizes prion formation in yeast","volume":"9","author":"Amor","year":"2015","journal-title":"Prion"},{"key":"2021070806054974900_iyab037-B2","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/1741-7007-4-32","article-title":"Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system","volume":"4","author":"Bagriantsev","year":"2006","journal-title":"BMC Biol"},{"key":"2021070806054974900_iyab037-B3","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1111\/mmi.13697","article-title":"To CURe or not to CURe? 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