{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kesari AS"],"funding":["NIAID NIH HHS","NIH HHS"],"pagination":["37"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7709110"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(4)"],"pubmed_abstract":["Proximity biotinylation was developed to detect physiologically relevant protein-protein interactions in living cells. In this method, the protein of interest is tagged with a promiscuous biotin ligase, such as BioID or BioID2, which produces activated biotin that reacts with nearby proteins; these proteins can subsequently be purified and identified by mass spectrometry. Here we report a novel modification of this technique by combining it with a self-associating split-GFP system in which we exploit the high-affinity interaction between GFP1-10 and GFP11 to recruit BioID2 to the protein of interest. As a test case, we fused GFP11 to clathrin light chain (CLTB) and BioID2 to GFP1-10. Co-expression of GFP11-CLTB and BioID2-GFP1-10 yielded a green fluorescent complex that co-localized with c"],"journal":["Proteomes"],"pubmed_title":["A Novel Proximity Biotinylation Assay Based on the Self-Associating Split GFP1-10/11."],"pmcid":["PMC7709110"],"funding_grant_id":["AI114814","P01 AI120943","AI120943","R01 AI114814"],"pubmed_authors":["LaCount DJ","Aryal UK","Kesari AS"],"additional_accession":[]},"is_claimable":false,"name":"A Novel Proximity Biotinylation Assay Based on the Self-Associating Split GFP1-10/11.","description":"Proximity biotinylation was developed to detect physiologically relevant protein-protein interactions in living cells. In this method, the protein of interest is tagged with a promiscuous biotin ligase, such as BioID or BioID2, which produces activated biotin that reacts with nearby proteins; these proteins can subsequently be purified and identified by mass spectrometry. Here we report a novel modification of this technique by combining it with a self-associating split-GFP system in which we exploit the high-affinity interaction between GFP1-10 and GFP11 to recruit BioID2 to the protein of interest. As a test case, we fused GFP11 to clathrin light chain (CLTB) and BioID2 to GFP1-10. Co-expression of GFP11-CLTB and BioID2-GFP1-10 yielded a green fluorescent complex that co-localized with c","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2025-04-04T19:21:23.027Z","creation":"2025-04-04T19:21:23.027Z"},"accession":"S-EPMC7709110","cross_references":{"pubmed":["33276494"],"doi":["10.3390/proteomes8040037"]}}