{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T00:34:39Z","timestamp":1792802079590,"version":"4.5.0"},"update-to":[{"DOI":"10.12688\/f1000research.15829.1","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2018,11,26]],"date-time":"2018-11-26T00:00:00Z","timestamp":1543190400000}}],"reference-count":30,"publisher":"F1000 Research Ltd","license":[{"start":{"date-parts":[[2018,11,26]],"date-time":"2018-11-26T00:00:00Z","timestamp":1543190400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["MOP-325538"],"award-info":[{"award-number":["MOP-325538"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"name":"The University of Western Ontario","id":[{"id":"https:\/\/ror.org\/02grkyz14","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":["f1000research.com"],"crossmark-restriction":false},"short-container-title":["F1000Res"],"abstract":"<ns4:p>\n                    Development of fluorescent proteins (FPs) enabled researchers to visualize protein localization and trafficking in living cells and organisms. The extended palette of available FPs allows simultaneous detection of multiple fluorescent fusion proteins. Importantly, FPs are originally derived from different organisms from jelly fish to corals and each FP displays its own biophysical properties. Among these properties, the tendency of FPs to oligomerize inherently affects the behavior of its fusion partner. Here we employed the budding yeast\n                    <ns4:italic>Saccharomyces cerevisiae<\/ns4:italic>\n                    to determine the impact of the latest generation of red FPs on their binding partner. We used a yeast assay based on the aggregation and toxicity of misfolded polyQ expansion proteins linked to Huntington\u2019s disease. Since polyQ aggregation and toxicity are highly dependent on the sequences flanking the polyQ region, polyQ expansions provide an ideal tool to assess the impact of FPs on their fusion partners. We found that unlike what is observed for green FP variants, yemRFP and yFusionRed-tagged polyQ expansions\u00a0 show reduced toxicity. \u00a0However, polyQ expansions tagged with the bright synthetically engineered ymScarlet displayed severe polyQ toxicity. Our data indicate that ymScarlet might have significant advantages over the previous generation of red FPs for use in fluorescent fusions in yeast.\n                  <\/ns4:p>","DOI":"10.12688\/f1000research.15829.2","type":"journal-article","created":{"date-parts":[[2018,11,26]],"date-time":"2018-11-26T11:50:10Z","timestamp":1543233010000},"page":"1242","update-policy":"https:\/\/doi.org\/10.12688\/f1000research.crossmark-policy","source":"Crossref","is-referenced-by-count":8,"title":["Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in Saccharomyces cerevisiae"],"prefix":"10.12688","volume":"7","author":[{"given":"Maram B.","family":"Albakri","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuwei","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie","family":"Genereaux","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1614-176X","authenticated-orcid":false,"given":"Patrick","family":"Lajoie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"2560","published-online":{"date-parts":[[2018,11,26]]},"reference":[{"key":"ref-1","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.12688\/f1000research.15829.2","article-title":"Dataset 1 in: Polyglutamine toxicity assays highlight the advantages of mScarlet for imaging in Saccharomyces cerevisiae.","volume":"7","author":"M Albakri","year":"2018","journal-title":"F1000Research."},{"key":"ref-2","doi-asserted-by":"publisher","first-page":"11984-11989","DOI":"10.1073\/pnas.97.22.11984","article-title":"Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral.","volume":"97","author":"G Baird","year":"2000","journal-title":"Proc Natl Acad Sci U S A."},{"key":"ref-3","doi-asserted-by":"publisher","first-page":"53-56","DOI":"10.1038\/nmeth.4074","article-title":"mScarlet: a bright monomeric red fluorescent protein for cellular imaging.","volume":"14","author":"D Bindels","year":"2017","journal-title":"Nat Methods."},{"key":"ref-4","doi-asserted-by":"publisher","first-page":"7877-7882","DOI":"10.1073\/pnas.082243699","article-title":"A monomeric red fluorescent protein.","volume":"99","author":"R Campbell","year":"2002","journal-title":"Proc Natl Acad Sci U S 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aggregation.","volume":"1017","author":"M Duennwald","year":"2013","journal-title":"Methods Mol Biol."},{"key":"ref-9","doi-asserted-by":"publisher","first-page":"11045-11050","DOI":"10.1073\/pnas.0604547103","article-title":"Flanking sequences profoundly alter polyglutamine toxicity in yeast.","volume":"103","author":"M Duennwald","year":"2006","journal-title":"Proc Natl Acad Sci U S A."},{"key":"ref-40","doi-asserted-by":"publisher","first-page":"11045-11050","DOI":"10.1073\/pnas.0604547103","article-title":"Flanking sequences profoundly alter polyglutamine toxicity in yeast.","volume":"103","author":"M Duennwald","year":"2006","journal-title":"Proc Natl Acad Sci U S A."},{"key":"ref-10","doi-asserted-by":"publisher","first-page":"656-662","DOI":"10.1016\/0959-4388(95)80072-7","article-title":"Huntington\u2019s disease: CAG genetics expands neurobiology.","volume":"5","author":"J Gusella","year":"1995","journal-title":"Curr Opin Neurobiol."},{"key":"ref-11","first-page":"317-321","article-title":"On Chorea.","volume":"26","author":"G Huntington","year":"1872","journal-title":"Medical and Surgical Reporter of Philadelphia."},{"key":"ref-12","doi-asserted-by":"publisher","first-page":"58-70","DOI":"10.1111\/tra.12453","article-title":"Polyglutamine toxicity in yeast uncovers phenotypic variations between different fluorescent protein fusions.","volume":"18","author":"Y Jiang","year":"2017","journal-title":"Traffic."},{"key":"ref-13","doi-asserted-by":"publisher","first-page":"705-710","DOI":"10.1534\/genetics.108.087080","article-title":"A new purple fluorescent color marker for genetic studies in Saccharomyces cerevisiae and Candida albicans.","volume":"179","author":"S Keppler-Ross","year":"2008","journal-title":"Genetics."},{"key":"ref-14","doi-asserted-by":"publisher","first-page":"1589-1594","DOI":"10.1073\/pnas.97.4.1589","article-title":"Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.","volume":"97","author":"S Krobitsch","year":"2000","journal-title":"Proc Natl Acad Sci U S A."},{"key":"ref-15","doi-asserted-by":"publisher","first-page":"e67902","DOI":"10.1371\/journal.pone.0067902","article-title":"Improved blue, green, and red fluorescent protein tagging vectors for S. cerevisiae.","volume":"8","author":"S Lee","year":"2013","journal-title":"PLos One."},{"key":"ref-16","doi-asserted-by":"publisher","first-page":"269-276","DOI":"10.4161\/pri.18005","article-title":"Modeling Huntington disease in yeast: perspectives and future directions.","volume":"5","author":"R Mason","year":"2011","journal-title":"Prion."},{"key":"ref-17","doi-asserted-by":"publisher","first-page":"997-1004","DOI":"10.1083\/jcb.200112104","article-title":"Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1.","volume":"157","author":"A Meriin","year":"2002","journal-title":"J Cell Biol."},{"key":"ref-18","doi-asserted-by":"publisher","first-page":"555-557","DOI":"10.1038\/nmeth1062","article-title":"Bright monomeric red fluorescent protein with an extended fluorescence lifetime.","volume":"4","author":"E Merzlyak","year":"2007","journal-title":"Nat Methods."},{"key":"ref-19","doi-asserted-by":"publisher","first-page":"119-122","DOI":"10.1016\/0378-1119(95)00037-7","article-title":"Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds.","volume":"156","author":"D Mumberg","year":"1995","journal-title":"Gene."},{"key":"ref-20","doi-asserted-by":"publisher","first-page":"689-692","DOI":"10.1002\/ana.410410521","article-title":"CAG repeat number governs the development rate of pathology in Huntington\u2019s disease.","volume":"41","author":"J Penney","year":"1997","journal-title":"Ann 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status","group":{"name":"current-referee-status","label":"Current Referee Status"}},{"value":"10.5256\/f1000research.17889.r41113, Danny M. Hatters, Dept of Biochem & Mol Biology, The University of Melbourne, Melbourne, VIC, 3010, Australia, 07 Dec 2018, version 2, indexed","URL":"https:\/\/f1000research.com\/articles\/7-1242\/v2#referee-response-41113","order":0,"name":"referee-response-41113","label":"Referee Report","group":{"name":"article-reports","label":"Article Reports"}},{"value":"10.5256\/f1000research.17889.r41114, Fedor V. Subach, Moscow Institute of Physics and Technology  (MIPT), Moscow, Russian Federation, 27 Nov 2018, version 2, indexed","URL":"https:\/\/f1000research.com\/articles\/7-1242\/v2#referee-response-41114","order":1,"name":"referee-response-41114","label":"Referee Report","group":{"name":"article-reports","label":"Article Reports"}},{"value":"This study was supported by an operating grant (MOP-325538) from the Canadian Institutes for Health Research (CIHR). YJ is supported by a M.Sc. to Ph.D. transfer scholarship from the Dean of the Schulich School of Medicine and Dentistry at The University of Western Ontario. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.","order":2,"name":"grant-information","label":"Grant Information"},{"value":"This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.Data associated with the article are available under the terms of the Creative Commons Zero \"No rights reserved\" data waiver (CC0 1.0 Public domain dedication).","order":0,"name":"copyright-info","label":"Copyright"}]}}