Fig. 4
Recombinant HtrA’s/DegP’s are proteolytically active and cleave E-cadherin in vitro. a Domain architecture of HtrA/DegP, DegQ and DegS proteins. SP, signal peptide (orange); protease domain (green); PDZ domains (purple); TMD, transmembrane domain (red). b The proteolytic activity of recombinant HtrA/DegP (rHtrA) wildtype proteins (wt) of H. pylori (Hp), S. Typhimurium (St), Y. enterocolitica (Ye), EPEC (Ep) and DegQ of P. mirabilis (Pm) was analyzed by casein zymography and compared to their corresponding inactive mutants (SA) (upper panel). Coomassie-stained SDS PAGEs demonstrated equal protein loading (lower panel). Self-processed proteins (black asterisks) exhibiting proteolytic activity (white asterisks) are indicated. c Recombinant HtrAs/DegPs (wt) were investigated in in vitro cleavage assays using E-cadherin (E-cadFL) as a substrate and compared with the corresponding inactive variants (SA) as a control. Fragments of E-cadherin were detected using an antibody recognizing the extracellular domain domain. HtrA/DegP proteins were detected using corresponding polyclonal antibodies