{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Stolle DS"],"funding":["Deutsche Forschungsgemeinschaft (DFG)","Deutsche Forschungsgemeinschaft","Max Planck Society"],"pagination":["4699-4719"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11480477"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(20)"],"pubmed_abstract":["Chloroplast-encoded multi-span thylakoid membrane proteins are crucial for photosynthetic complexes, yet the coordination of their biogenesis remains poorly understood. To identify factors that specifically support the cotranslational biogenesis of the reaction center protein D1 of photosystem (PS) II, we generated and affinity-purified stalled ribosome-nascent chain complexes (RNCs) bearing D1 nascent chains. Stalled RNCs translating the soluble ribosomal subunit uS2c were used for comparison. Quantitative tandem-mass spectrometry of the purified RNCs identified around 140 proteins specifically associated with D1 RNCs, mainly involved in protein and cofactor biogenesis, including chlorophyll biosynthesis, and other metabolic pathways. Functional analysis of STIC2, a newly identified D1 RN"],"journal":["The EMBO journal"],"pubmed_title":["STIC2 selectively binds ribosome-nascent chain complexes in the cotranslational sorting of Arabidopsis thylakoid proteins."],"pmcid":["PMC11480477"],"funding_grant_id":["ZO 302/5-1","BA 1902/2-2","836/3-2","SCHU 1163/6-2"],"pubmed_authors":["Karstens M","Osterhoff L","Treimer P","Baginsky S","Herrmann C","Bischoff A","Schunemann D","Stolle DS","Keller JM","Hofmann E","Lambertz J","Dunschede B","Armbruster U","Rodiger A","Zoschke R","Nowaczyk MM","Gerlach I"],"additional_accession":[]},"is_claimable":false,"name":"STIC2 selectively binds ribosome-nascent chain complexes in the cotranslational sorting of Arabidopsis thylakoid proteins.","description":"Chloroplast-encoded multi-span thylakoid membrane proteins are crucial for photosynthetic complexes, yet the coordination of their biogenesis remains poorly understood. To identify factors that specifically support the cotranslational biogenesis of the reaction center protein D1 of photosystem (PS) II, we generated and affinity-purified stalled ribosome-nascent chain complexes (RNCs) bearing D1 nascent chains. Stalled RNCs translating the soluble ribosomal subunit uS2c were used for comparison. Quantitative tandem-mass spectrometry of the purified RNCs identified around 140 proteins specifically associated with D1 RNCs, mainly involved in protein and cofactor biogenesis, including chlorophyll biosynthesis, and other metabolic pathways. Functional analysis of STIC2, a newly identified D1 RN","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-15T13:03:02.093Z","creation":"2025-04-04T23:50:20.535Z"},"accession":"S-EPMC11480477","cross_references":{"pubmed":["39192033"],"doi":["10.1038/s44318-024-00211-4"]}}