{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Salerno-Kochan A"],"funding":["IIMCB Statutory Funds","German Research Foundation","Foundation for Polish Science","National Science Centre","German Federal Ministry of Education and Research","European Union’s Horizon 2020 research and innovation programme"],"pagination":["e202201418"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9070667"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(8)"],"pubmed_abstract":["The TRIM-NHL protein Meiotic P26 (Mei-P26) acts as a regulator of cell fate in <i>Drosophila</i> Its activity is critical for ovarian germline stem cell maintenance, differentiation of oocytes, and spermatogenesis. Mei-P26 functions as a post-transcriptional regulator of gene expression; however, the molecular details of how its NHL domain selectively recognizes and regulates its mRNA targets have remained elusive. Here, we present the crystal structure of the Mei-P26 NHL domain at 1.6 Å resolution and identify key amino acids that confer substrate specificity and distinguish Mei-P26 from closely related TRIM-NHL proteins. Furthermore, we identify mRNA targets of Mei-P26 in cultured <i>Drosophila</i> cells and show that Mei-P26 can act as either a repressor or activator of gene expression "],"journal":["Life science alliance"],"pubmed_title":["Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26."],"pmcid":["PMC9070667"],"funding_grant_id":["UMO-2015/19/P/NZ1/02514","665778","01ZX1401D","2017/26/A/NZ1/01083","TECH CORE FACILITY/2017-4/6","SFB960 TP B11, ME4238/1-1","UMO-2019/32/T/NZ1/00420","TEAM/2016-3/18","RTG2355 325443116"],"pubmed_authors":["Medenbach J","Koscielniak A","Strauss D","Bujnicki JM","Krutyholowa R","Horn A","Salerno-Kochan A","Nithin C","Rossbach O","Ghosh P","Gaik M","Glatt S","Meindl A"],"additional_accession":[]},"is_claimable":false,"name":"Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26.","description":"The TRIM-NHL protein Meiotic P26 (Mei-P26) acts as a regulator of cell fate in <i>Drosophila</i> Its activity is critical for ovarian germline stem cell maintenance, differentiation of oocytes, and spermatogenesis. Mei-P26 functions as a post-transcriptional regulator of gene expression; however, the molecular details of how its NHL domain selectively recognizes and regulates its mRNA targets have remained elusive. Here, we present the crystal structure of the Mei-P26 NHL domain at 1.6 Å resolution and identify key amino acids that confer substrate specificity and distinguish Mei-P26 from closely related TRIM-NHL proteins. Furthermore, we identify mRNA targets of Mei-P26 in cultured <i>Drosophila</i> cells and show that Mei-P26 can act as either a repressor or activator of gene expression ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-05-31T20:59:16.672Z","creation":"2025-02-19T04:20:58.653Z"},"accession":"S-EPMC9070667","cross_references":{"pubmed":["35512835"],"doi":["10.26508/lsa.202201418"]}}