{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Panwar HS"],"funding":["NIGMS NIH HHS"],"pubmed_abstract":["H/ACA small nucleolar ribonucleoproteins (H/ACA snoRNPs) facilitate essential cellular processes such as RNA modification, folding, and stability. Here, we present multiple cryo-EM structures of endogenous, catalytically active insect H/ACA snoRNPs containing two protomers assembled on a two-hairpin H/ACA snoRNA. By characterizing key protein-protein and protein-RNA interactions, we reveal the coordination of pseudouridylation activity across the two protomers which explains the predominance of two-hairpin structures in eukaryotic H/ACA snoRNAs. Moreover, we discovered that several mutations in H/ACA proteins associated with Dyskeratosis congenita directly impair pseudouridine formation suggesting how these mutations disrupt RNA modification and ribosome biogenesis in this disease. Additio"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.06.07.658439"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12157440"],"repository":["biostudies-literature"],"pubmed_title":["Interprotomer Communication and Functional Asymmetry in H/ACA snoRNPs."],"pmcid":["PMC12157440"],"funding_grant_id":["R35 GM147261"],"pubmed_authors":["Kothe U","Xie X","Sheldon R","Lee H","Jang HS","Worden E","Vos TJ","Panwar HS"],"additional_accession":[]},"is_claimable":false,"name":"Interprotomer Communication and Functional Asymmetry in H/ACA snoRNPs.","description":"H/ACA small nucleolar ribonucleoproteins (H/ACA snoRNPs) facilitate essential cellular processes such as RNA modification, folding, and stability. Here, we present multiple cryo-EM structures of endogenous, catalytically active insect H/ACA snoRNPs containing two protomers assembled on a two-hairpin H/ACA snoRNA. By characterizing key protein-protein and protein-RNA interactions, we reveal the coordination of pseudouridylation activity across the two protomers which explains the predominance of two-hairpin structures in eukaryotic H/ACA snoRNAs. Moreover, we discovered that several mutations in H/ACA proteins associated with Dyskeratosis congenita directly impair pseudouridine formation suggesting how these mutations disrupt RNA modification and ribosome biogenesis in this disease. Additio","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-04-08T19:34:18.35Z","creation":"2026-04-08T13:59:10.933Z"},"accession":"S-EPMC12157440","cross_references":{"pubmed":["40501553"],"doi":["10.1101/2025.06.07.658439"]}}