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Microbiology 152 (2006), 1441-1450; DOI  10.1099/mic.0.28734-0
© 2006 Society for General Microbiology

Surface plasmon resonance-based interaction studies reveal competition of Streptomyces lividans type I signal peptidases for binding preproteins

Nick Geukens1, Smitha Rao C. V.1, Rafael P. Mellado2, Filip Frederix3, Gunter Reekmans3, Sophie De Keersmaeker1, Kristof Vrancken1, Kristien Bonroy3, Lieve Van Mellaert1, Elke Lammertyn1 and Jozef Anné1

1 Laboratory of Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium
2 Department of Microbial Biotechnology, Centro Nacional de Biotecnologia, Campus de la Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain
3 IMEC, MCP-ART, Kapeldreef 75, B-3001 Leuven, Belgium

Correspondence
Jozef Anné
Jozef.Anne{at}rega.kuleuven.be

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.

Abbreviations: SPase, type I signal peptidase; SPR, surface plasmon resonance; Tat, twin-arginine translocation




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S. De Keersmaeker, K. Vrancken, L. Van Mellaert, J. Anne, and N. Geukens
The Tat pathway in Streptomyces lividans: interaction of Tat subunits and their role in translocation
Microbiology, April 1, 2007; 153(4): 1087 - 1094.
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