<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Du M</submitter><funding>Guangdong Innovative and Entrepreneurial Research Team Program</funding><funding>Guangdong Program</funding><funding>Guangdong Basic and Applied Basic Research Foundation</funding><funding>National Natural Science Foundation of China</funding><funding>Shenzhen Science and Technology Program</funding><pagination>7947-7960</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11260487</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>52(13)</volume><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</pubmed_abstract><journal>Nucleic acids research</journal><pubmed_title>YjgA plays dual roles in enhancing PTC maturation.</pubmed_title><pmcid>PMC11260487</pmcid><funding_grant_id>2021ZT09Y104</funding_grant_id><funding_grant_id>2021A1515010805</funding_grant_id><funding_grant_id>2021QN02Y353</funding_grant_id><funding_grant_id>32171200</funding_grant_id><funding_grant_id>JCYJ20220530115210023</funding_grant_id><funding_grant_id>92169111</funding_grant_id><pubmed_authors>Deng C</pubmed_authors><pubmed_authors>Zhou Q</pubmed_authors><pubmed_authors>Yu T</pubmed_authors><pubmed_authors>Zeng F</pubmed_authors><pubmed_authors>Du M</pubmed_authors></additional><is_claimable>false</is_claimable><name>YjgA plays dual roles in enhancing PTC maturation.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Jul</publication><modification>2026-06-01T20:36:56.746Z</modification><creation>2025-05-18T13:26:19.816Z</creation></dates><accession>S-EPMC11260487</accession><cross_references><pubmed>38842932</pubmed><doi>10.1093/nar/gkae469</doi></cross_references></HashMap>