{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":48,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["10(2)"],"submitter":["Zhou D"],"pubmed_abstract":["Assembly of eukaryotic ribosome is a complicated and dynamic process that involves a series of intermediates. It is unknown how the highly intertwined structure of 60S large ribosomal subunits is established. Here, we report the structure of an early nucleolar pre-60S ribosome determined by cryo-electron microscopy at 3.7 Å resolution, revealing a half-assembled subunit. Domains I, II and VI of 25S/5.8S rRNA pack tightly into a native-like substructure, but domains III, IV and V are not assembled. The structure contains 12 assembly factors and 19 ribosomal proteins, many of which are required for early processing of large subunit rRNA. The Brx1-Ebp2 complex would interfere with the assembly of domains IV and V. Rpf1, Mak16, Nsa1 and Rrp1 form a cluster that consolidates the joining of domains I and II. Our structure reveals a key intermediate on the path to establishing the global architecture of 60S subunits."],"journal":["Protein & cell"],"pagination":["120-130"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6340896"],"repository":["biostudies-literature"],"pubmed_title":["Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate."],"pmcid":["PMC6340896"],"pubmed_authors":["Zheng S","Tan D","Zhou D","Zhu X","Ye K","Dong MQ"],"view_count":["48"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate.","description":"Assembly of eukaryotic ribosome is a complicated and dynamic process that involves a series of intermediates. It is unknown how the highly intertwined structure of 60S large ribosomal subunits is established. Here, we report the structure of an early nucleolar pre-60S ribosome determined by cryo-electron microscopy at 3.7 Å resolution, revealing a half-assembled subunit. Domains I, II and VI of 25S/5.8S rRNA pack tightly into a native-like substructure, but domains III, IV and V are not assembled. The structure contains 12 assembly factors and 19 ribosomal proteins, many of which are required for early processing of large subunit rRNA. The Brx1-Ebp2 complex would interfere with the assembly of domains IV and V. Rpf1, Mak16, Nsa1 and Rrp1 form a cluster that consolidates the joining of domains I and II. Our structure reveals a key intermediate on the path to establishing the global architecture of 60S subunits.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Feb","modification":"2024-11-09T01:22:59.907Z","creation":"2019-03-26T22:53:11Z"},"accession":"S-EPMC6340896","cross_references":{"pubmed":["29557065"],"doi":["10.1007/s13238-018-0526-7"]}}