Fig. 2From: A Chlamydia trachomatis strain with a chemically generated amino acid substitution (P370L) in the cthtrA gene shows reduced elementary body productionIn vitro biochemical activity of wild type C. trachomatis L2 and recombinant mutants. a. Cleavage of full-length β-casein by wild type CtHtrA and recombinant mutants over a 60 min time course. The corresponding SDS-PAGE gels are provided in Additional file 2: Figure S1. b. Rate of proteolysis of the βcas1 peptide substrate with and without allosteric activation (Act1 peptide) by recombinant proteins. Numbers above the bars represent the fold-change in proteolytic activity following the addition of the Act1 activator. Rate of proteolysis is measured as μM MCA min−1 μg CtHtrA−1. Error bars represent standard error of the mean (n = 6). c. Measurement of the proteolytic activity of wild type CtHtrA and mutants in the presence of pNA1-4 peptide substrates. Rate of proteolysis is measured as pNA 405 nm min−1. Error bars represent standard error of the mean (n = 6). d. Wild type CtHtrA and the mutants oligomerise to 24-mer in the presence of full-length β-casein. The figure shows glutaraldehyde crosslinked protein samples prepared by oligomerisation assays following separation on 3–8 % TrisAcetate gels prior to silver staining. The size of the 24-meric oligomer is indicated to the right of the gel and the molecular weights are indicated on the left (High Molecular Weight Marker, Invitrogen)Back to article page