{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Du M"],"funding":["Guangdong Innovative and Entrepreneurial Research Team Program","Guangdong Program","Guangdong Basic and Applied Basic Research Foundation","National Natural Science Foundation of China","Shenzhen Science and Technology Program"],"pagination":["7947-7960"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11260487"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52(13)"],"pubmed_abstract":["Ribosome biogenesis is a highly regulated cellular process that involves the control of numerous assembly factors. The small protein YjgA has been reported to play a role in the late stages of 50S assembly. However, the precise molecular mechanism underlying its function remains unclear. In this study, cryo-electron microscopy (cryo-EM) structures revealed that depletion of YjgA or its N-terminal loop in Escherichia coli both lead to the accumulation of immature 50S particles with structural abnormalities mainly in peptidyl transferase center (PTC) and H68/69 region. CryoDRGN analysis uncovered 8 and 6 distinct conformations of pre50S for ΔyjgA and YjgA-ΔNloop, respectively. These conformations highlighted the role of the N-terminal loop of YjgA in integrating uL16 and stabilizing H89 in P"],"journal":["Nucleic acids research"],"pubmed_title":["YjgA plays dual roles in enhancing PTC maturation."],"pmcid":["PMC11260487"],"funding_grant_id":["2021ZT09Y104","2021A1515010805","2021QN02Y353","32171200","JCYJ20220530115210023","92169111"],"pubmed_authors":["Deng C","Zhou Q","Yu T","Zeng F","Du M"],"additional_accession":[]},"is_claimable":false,"name":"YjgA plays dual roles in enhancing PTC maturation.","description":"Ribosome biogenesis is a highly regulated cellular process that involves the control of numerous assembly factors. The small protein YjgA has been reported to play a role in the late stages of 50S assembly. However, the precise molecular mechanism underlying its function remains unclear. In this study, cryo-electron microscopy (cryo-EM) structures revealed that depletion of YjgA or its N-terminal loop in Escherichia coli both lead to the accumulation of immature 50S particles with structural abnormalities mainly in peptidyl transferase center (PTC) and H68/69 region. CryoDRGN analysis uncovered 8 and 6 distinct conformations of pre50S for ΔyjgA and YjgA-ΔNloop, respectively. These conformations highlighted the role of the N-terminal loop of YjgA in integrating uL16 and stabilizing H89 in P","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T20:36:56.746Z","creation":"2025-05-18T13:26:19.816Z"},"accession":"S-EPMC11260487","cross_references":{"pubmed":["38842932"],"doi":["10.1093/nar/gkae469"]}}