{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Izert-Nowakowska MA"],"funding":["Fundacja na rzecz Nauki Polskiej (FNP)","Ministerstwo Edukacji i Nauki (MNiSW)","Narodowe Centrum Nauki (NCN)"],"pagination":["3994-4016"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12373786"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(16)"],"pubmed_abstract":["New, universal tools for targeted protein degradation in bacteria can help to accelerate protein function studies and antimicrobial research. We describe a new method for degrading bacterial proteins using plasmid-encoded degrader peptides which deliver target proteins for degradation by a highly conserved ClpXP protease. We demonstrate the mode of action of the degraders on a challenging essential target, GroEL. The studies in bacteria are complemented by in vitro binding and structural studies. Expression of degrader peptides results in a temperature-dependent growth inhibition and depletion of GroEL levels over time. The reduction of GroEL levels is accompanied by dramatic proteome alterations. The presented method offers a new alternative approach for regulating protein levels in bacteria without genomic modifications or tag fusions. Our studies demonstrate that ClpXP is an attractive protease for the future use in bacterial-targeted protein degradation."],"journal":["EMBO reports"],"pubmed_title":["Targeted protein degradation in Escherichia coli using CLIPPERs."],"pmcid":["PMC12373786"],"funding_grant_id":["Initiative of Excellence - Research University,University of Warsaw I.4.1&2,BOB-IDUB-622-20/2021","2020/39/B/NZ2/01301","POIR.04.04.00-00-5EC1/18-00"],"pubmed_authors":["Wroblewski K","Kowalski JJ","Goral T","Kmiecik S","Klimecka MM","Bandyra KJ","Gorna MW","Antosiewicz A","Serwa RA","Izert-Nowakowska MA"],"additional_accession":[]},"is_claimable":false,"name":"Targeted protein degradation in Escherichia coli using CLIPPERs.","description":"New, universal tools for targeted protein degradation in bacteria can help to accelerate protein function studies and antimicrobial research. We describe a new method for degrading bacterial proteins using plasmid-encoded degrader peptides which deliver target proteins for degradation by a highly conserved ClpXP protease. We demonstrate the mode of action of the degraders on a challenging essential target, GroEL. The studies in bacteria are complemented by in vitro binding and structural studies. Expression of degrader peptides results in a temperature-dependent growth inhibition and depletion of GroEL levels over time. The reduction of GroEL levels is accompanied by dramatic proteome alterations. The presented method offers a new alternative approach for regulating protein levels in bacteria without genomic modifications or tag fusions. Our studies demonstrate that ClpXP is an attractive protease for the future use in bacterial-targeted protein degradation.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-09T10:46:43.109Z","creation":"2026-04-08T00:48:54.807Z"},"accession":"S-EPMC12373786","cross_references":{"pubmed":["40562793"],"doi":["10.1038/s44319-025-00510-9"]}}