<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>113(21)</volume><submitter>Chakrabortee S</submitter><pubmed_abstract>Prion proteins provide a unique mode of biochemical memory through self-perpetuating changes in protein conformation and function. They have been studied in fungi and mammals, but not yet identified in plants. Using a computational model, we identified candidate prion domains (PrDs) in nearly 500 plant proteins. Plant flowering is of particular interest with respect to biological memory, because its regulation involves remembering and integrating previously experienced environmental conditions. We investigated the prion-forming capacity of three prion candidates involved in flowering using a yeast model, where prion attributes are well defined and readily tested. In yeast, prions heritably change protein functions by templating monomers into higher-order assemblies. For most yeast prions, </pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pagination>6065-70</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4889399</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Luminidependens (LD) is an Arabidopsis protein with prion behavior.</pubmed_title><pmcid>PMC4889399</pmcid><pubmed_authors>Chakrabortee S</pubmed_authors><pubmed_authors>Lindquist S</pubmed_authors><pubmed_authors>Kayatekin C</pubmed_authors><pubmed_authors>Mendillo ML</pubmed_authors><pubmed_authors>Lancaster A</pubmed_authors><pubmed_authors>Newby GA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Luminidependens (LD) is an Arabidopsis protein with prion behavior.</name><description>Prion proteins provide a unique mode of biochemical memory through self-perpetuating changes in protein conformation and function. They have been studied in fungi and mammals, but not yet identified in plants. Using a computational model, we identified candidate prion domains (PrDs) in nearly 500 plant proteins. Plant flowering is of particular interest with respect to biological memory, because its regulation involves remembering and integrating previously experienced environmental conditions. We investigated the prion-forming capacity of three prion candidates involved in flowering using a yeast model, where prion attributes are well defined and readily tested. In yeast, prions heritably change protein functions by templating monomers into higher-order assemblies. For most yeast prions, </description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 May</publication><modification>2025-04-05T12:02:00.24Z</modification><creation>2019-03-27T02:15:01Z</creation></dates><accession>S-EPMC4889399</accession><cross_references><pubmed>27114519</pubmed><doi>10.1073/pnas.1604478113</doi></cross_references></HashMap>