Proteome dysregulation induced by degrader peptides targeting GroEL chaperone in Escherichia coli

Inducible degradation presents an attractive alternative for modulating protein levels in bacteria without genome editing or RNA interference. In this work we constructed a series of plasmids encoding degrader peptides which bring together an essential GroEL chaperone and activated ClpXP protease to trigger GroEL degradation. Escherichia coli BW25113 was transformed with studied and control plasmids. The effect of peptide expression on bacterial proteome was monitored in thermal stress (42 °C) by TMT-MS in three time points to confirm GroEL degradation and secondary effects on bacterial proteome arising from target depletion.