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Volume 152, Issue 5

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

Abstract

Type I signal peptidases (SPases) are responsible for the cleavage of signal peptides from secretory proteins. contains four different SPases, denoted SipW, SipX, SipY and SipZ, having at least some differences in their substrate specificity. In this report 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 assay, suggested that there is no real specificity in substrate binding and processing, and that they are all actively involved in preprotein processing . 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 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 .

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Keyword(s): SPase, type I signal peptidase , SPR, surface plasmon resonance and Tat, twin-arginine translocation
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2006-05-01
2024-04-19
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Surface plasmon resonance-based interaction studies reveal competition of Streptomyces lividans type I signal peptidases for binding preproteins
Microbiology 152, 1441 (2006); https://doi.org/10.1099/mic.0.28734-0
/content/journal/micro/10.1099/mic.0.28734-0
/content/journal/micro/10.1099/mic.0.28734-0
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