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Fig. 2 | BMC Microbiology

Fig. 2

From: A Chlamydia trachomatis strain with a chemically generated amino acid substitution (P370L) in the cthtrA gene shows reduced elementary body production

Fig. 2

In 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)

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