{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Beard HA"],"funding":["RCUK | Biotechnology and Biological Sciences Research Council","RCUK | Engineering and Physical Sciences Research Council","Wellcome Trust","Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["133"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7610391"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["2"],"pubmed_abstract":["Ligand-directed protein labelling allows the introduction of diverse chemical functionalities onto proteins without the need for genetically encoded tags. Here we report a method for the rapid labelling of a protein using a ruthenium-bipyridyl (Ru(II)(bpy)<sub>3</sub>)-modified peptide designed to mimic an interacting BH3 ligand within a BCL-2 family protein-protein interactions. Using sub-stoichiometric quantities of (Ru(II)(bpy)<sub>3</sub>)-modified NOXA-B and irradiation with visible light for 1 min, the anti-apoptotic protein MCL-1 can be photolabelled with a variety of functional tags. In contrast with previous reports on Ru(II)(bpy)<sub>3</sub>-mediated photolabelling, tandem mass spectrometry experiments reveal that the labelling site is a cysteine residue of MCL-1. MCL-1 can be la"],"journal":["Communications chemistry"],"pubmed_title":["Photocatalytic proximity labelling of MCL-1 by a BH3 ligand."],"pmcid":["PMC7610391"],"funding_grant_id":["097827/Z/11/A","094232","BB/M012573/1","EP/KO39292/1","094232/Z/10/Z","EP/N013573","EPSRC DTA","097827","1512523","WT094232MA","EP/N013573/1"],"pubmed_authors":["Beard HA","Walko M","George RM","Wilson AJ","Bon RS","Hauser JR"],"additional_accession":[]},"is_claimable":false,"name":"Photocatalytic proximity labelling of MCL-1 by a BH3 ligand.","description":"Ligand-directed protein labelling allows the introduction of diverse chemical functionalities onto proteins without the need for genetically encoded tags. Here we report a method for the rapid labelling of a protein using a ruthenium-bipyridyl (Ru(II)(bpy)<sub>3</sub>)-modified peptide designed to mimic an interacting BH3 ligand within a BCL-2 family protein-protein interactions. Using sub-stoichiometric quantities of (Ru(II)(bpy)<sub>3</sub>)-modified NOXA-B and irradiation with visible light for 1 min, the anti-apoptotic protein MCL-1 can be photolabelled with a variety of functional tags. In contrast with previous reports on Ru(II)(bpy)<sub>3</sub>-mediated photolabelling, tandem mass spectrometry experiments reveal that the labelling site is a cysteine residue of MCL-1. MCL-1 can be la","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Nov","modification":"2026-05-01T17:29:49.042Z","creation":"2024-11-13T06:29:58.89Z"},"accession":"S-EPMC7610391","cross_references":{"pubmed":["33763603"],"doi":["10.1038/s42004-019-0235-z"]}}