Abstract
Bacillus subtilis contains four closely related, chromosomally-encoded type I signal peptidases (SipS, SipT, SipU and SipV), which remove signal peptides from secretory precursor proteins. In the present studies, the role of SipS in protein secretion in B. subtilis was analysed. Interestingly, the absence of SipS had opposite effects on the secretion of different mature proteins into the growth medium. For example, the neutral protease NprE was secreted at reduced levels, whereas levansucrase was secreted at increased levels. Similarly, the processing of certain secretory precursor proteins was reduced, whereas processing of other precursors was improved. The latter observation indicates that the presence of SipS can interfere with efficient processing of certain precursor proteins, which raises the question whether the type I signal peptidases of B. subtilis compete for binding and cleavage of secretory precursor proteins.
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Bolhuis, A., Tjalsma, H., Venema, G., Bron, S., van Dijl, J.M. (1998). Do the Type I Signal Peptidases of Bacillus subtilis Compete for Binding and Cleavage of Secretory Precursor Proteins?. In: Op den Kamp, J.A.F. (eds) Lipid and Protein Traffic. NATO ASI Series, vol 106. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-51463-0_14
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DOI: https://doi.org/10.1007/978-3-642-51463-0_14
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