RT Journal Article SR Electronic(1) A1 Geukens, Nick A1 Rao C. V., Smitha A1 Mellado, Rafael P. A1 Frederix, Filip A1 Reekmans, Gunter A1 De Keersmaeker, Sophie A1 Vrancken, Kristof A1 Bonroy, Kristien A1 Van Mellaert, Lieve A1 Lammertyn, Elke A1 Anné, JozefYR 2006 T1 Surface plasmon resonance-based interaction studies reveal competition of Streptomyces lividans type I signal peptidases for binding preproteins JF Microbiology, VO 152 IS 5 SP 1441 OP 1450 DO https://doi.org/10.1099/mic.0.28734-0 PB Microbiology Society, SN 1465-2080, AB Type I signal peptidases (SPases) are responsible for the cleavage of signal peptides from secretory proteins. Streptomyces lividans contains four different SPases, denoted SipW, SipX, SipY and SipZ, having at least some differences in their substrate specificity. In this report in vitro preprotein binding/processing and protein secretion in single SPase mutants was determined to gain more insight into the substrate specificity of the different SPases and the underlying molecular basis. Results indicated that preproteins do not preferentially bind to a particular SPase, suggesting SPase competition for binding preproteins. This observation, together with the fact that each SPase could process each preprotein tested with a similar efficiency in an in vitro assay, suggested that there is no real specificity in substrate binding and processing, and that they are all actively involved in preprotein processing in vivo. Although this seems to be the case for some proteins tested, high-level secretion of others was clearly dependent on only one particular SPase demonstrating clear differences in substrate preference at the in vivo processing level. Hence, these results strongly suggest that there are additional factors other than the cleavage requirements of the enzymes that strongly affect the substrate preference of SPases in vivo., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.28734-0