{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,5]],"date-time":"2026-01-05T15:12:55Z","timestamp":1767625975975,"version":"3.37.3"},"reference-count":83,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2014,8,21]],"date-time":"2014-08-21T00:00:00Z","timestamp":1408579200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM072778"],"award-info":[{"award-number":["GM072778"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,9]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Molecular chaperones monitor protein homeostasis and defend against the misfolding and aggregation of proteins that is associated with protein conformational disorders. In these diseases, a variety of different aggregate structures can form. These are called prion strains, or variants, in prion diseases, and cause variation in disease pathogenesis. Here, we use variants of the yeast prions [<jats:styled-content style=\"fixed-case\"><jats:italic>RNQ<\/jats:italic><\/jats:styled-content>+] and [<jats:styled-content style=\"fixed-case\"><jats:italic>PSI<\/jats:italic><\/jats:styled-content>+] to explore the interactions of chaperones with distinct aggregate structures. We found that prion variants show striking variation in their relationship with <jats:styled-content style=\"fixed-case\">Hsp<\/jats:styled-content>40s. Specifically, the yeast <jats:styled-content style=\"fixed-case\">Hsp40 Sis1<\/jats:styled-content> and its human orthologue <jats:styled-content style=\"fixed-case\">Hdj1<\/jats:styled-content> had differential capacities to process prion variants, suggesting that <jats:styled-content style=\"fixed-case\">Hsp40<\/jats:styled-content> selectivity has likely changed through evolution. We further show that such selectivity involves different domains of <jats:styled-content style=\"fixed-case\">Sis1<\/jats:styled-content>, with some prion conformers having a greater dependence on particular <jats:styled-content style=\"fixed-case\">Hsp40<\/jats:styled-content> domains. Moreover, [<jats:styled-content style=\"fixed-case\"><jats:italic>PSI<\/jats:italic><\/jats:styled-content>+] variants were more sensitive to certain alterations in <jats:styled-content style=\"fixed-case\">Hsp70<\/jats:styled-content> activity as compared to [<jats:styled-content style=\"fixed-case\"><jats:italic>RNQ<\/jats:italic><\/jats:styled-content>+] variants. Collectively, our data indicate that distinct chaperone machinery is required, or has differential capacity, to process different aggregate structures. Elucidating the intricacies of chaperone\u2010client interactions, and how these are altered by particular client structures, will be crucial to understanding how this system can go awry in disease and contribute to pathological variation.<\/jats:p>","DOI":"10.1111\/mmi.12725","type":"journal-article","created":{"date-parts":[[2014,7,24]],"date-time":"2014-07-24T09:47:05Z","timestamp":1406195225000},"page":"1156-1171","source":"Crossref","is-referenced-by-count":23,"title":["Structural variants of yeast prions show conformer\u2010specific requirements for chaperone activity"],"prefix":"10.1111","volume":"93","author":[{"given":"Kevin C.","family":"Stein","sequence":"first","affiliation":[{"name":"Department of Cell Biology and Physiology Washington University School of Medicine  St. Louis MO 63110 USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Heather L.","family":"True","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Physiology 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