Abstract
The bacterial secretory pathway is responsible for the translocation of exported preproteins, and for the assembly of membrane preproteins. Signal peptidase I (SPase I) is responsible for the cleavage of the signal peptide from these preproteins. We have used tryptophan fluorescence spectroscopy of the soluble Escherichia coli SPase I Δ2-75 to study the dynamic conformational changes that occur when the enzyme is in solution and when interacting with lipids and the signal peptide. E. coli SPase I Δ2-75 has four tryptophan residues (W261, W284, W300 and W310).
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