{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Leydon AR"],"funding":["HHS | National Institutes of Health","Life Sciences Research Foundation","Howard Hughes Medical Institute","NIGMS NIH HHS"],"pagination":["e2206986119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9564828"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(41)"],"pubmed_abstract":["The corepressor TOPLESS (TPL) and its paralogs coordinately regulate a large number of genes critical to plant development and immunity. As in many members of the larger pan-eukaryotic Tup1/TLE/Groucho corepressor family, TPL contains a Lis1 Homology domain (LisH), whose function is not well understood. We have previously found that the LisH in TPL-and specifically the N-terminal 18 amino acid alpha-helical region (TPL-H1)-can act as an autonomous repression domain. We hypothesized that homologous domains across diverse LisH-containing proteins could share the same function. To test that hypothesis, we built a library of H1s that broadly sampled the sequence and evolutionary space of LisH domains, and tested their activity in a synthetic transcriptional repression assay in <i>Saccharomyces"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["A single helix repression domain is functional across diverse eukaryotes."],"pmcid":["PMC9564828"],"funding_grant_id":["NA","R01 GM107084","10115746"],"pubmed_authors":["Ramos Baez R","Nemhauser JL","Leydon AR"],"additional_accession":[]},"is_claimable":false,"name":"A single helix repression domain is functional across diverse eukaryotes.","description":"The corepressor TOPLESS (TPL) and its paralogs coordinately regulate a large number of genes critical to plant development and immunity. As in many members of the larger pan-eukaryotic Tup1/TLE/Groucho corepressor family, TPL contains a Lis1 Homology domain (LisH), whose function is not well understood. We have previously found that the LisH in TPL-and specifically the N-terminal 18 amino acid alpha-helical region (TPL-H1)-can act as an autonomous repression domain. We hypothesized that homologous domains across diverse LisH-containing proteins could share the same function. To test that hypothesis, we built a library of H1s that broadly sampled the sequence and evolutionary space of LisH domains, and tested their activity in a synthetic transcriptional repression assay in <i>Saccharomyces","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-07-14T19:05:47.861Z","creation":"2025-04-07T03:20:47.785Z"},"accession":"S-EPMC9564828","cross_references":{"pubmed":["36191192"],"doi":["10.1073/pnas.2206986119"]}}