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TitleTargeted protein degradation in Escherichia coli using CLIPPERs.
Journal, issue, pagesEMBO Rep, Vol. 26, Issue 16, Page 3994-4016, Year 2025
Publish dateJun 25, 2025
AuthorsMatylda Anna Izert-Nowakowska / Maria Magdalena Klimecka / Anna Antosiewicz / Karol Wróblewski / Jakub Józef Kowalski / Katarzyna Justyna Bandyra / Tomasz Góral / Sebastian Kmiecik / Remigiusz Adam Serwa / Maria Wiktoria Górna /
PubMed AbstractNew, 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 ...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.
External linksEMBO Rep / PubMed:40562793 / PubMed Central
MethodsEM (single particle)
Resolution2.45 Å
Structure data

19687

8s32

EMDB-19687, PDB-8s32:
GroEL with bound GroTAC peptide
Method: EM (single particle) / Resolution: 2.45 Å

Source
  • escherichia coli (E. coli)
  • synthetic construct (others)
KeywordsCHAPERONE / GroEL / GroTAC / PROTAC / degrader / complex

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