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Title: Physical requirements for in vitro processing of the Streptomyces lividans signal peptidases
Authors: Geukens, Nick ×
Lammertyn, Elke
Van Mellaert, Lieve
Engelborghs, Yves
Mellado, RP
Anné, Jozef #
Issue Date: Jan-2002
Publisher: Elsevier science bv
Series Title: Journal of biotechnology vol:96 issue:1 pages:79-91
Abstract: The Gram-positive eubacterium Streptomyces lividans contains four chromosomally encoded type I signal peptidases, SipW, SipX, SipY and SipZ, of which all but SipW have an unusual C-terminal membrane anchor. For in vitro characterisation of these signal peptidases, the S. lividans sip genes were expressed in Escherichia coli and the corresponding proteins were purified. The four enzymes had an optimum activity at an alkaline pH, notably pH 8-9 for SipW and SipY and pH 10-11 for SipX and SipZ. In contrast to SipW, the in vitro activities of SipX, SipY and SipZ significantly increased in the presence of detergent. Since none of the S. lividans Sip proteins contains the hydrophobic P-barrel domain, which in E. coli LepB was proven to be requisite for detergent-dependent in vitro activity, we assume that for detergent dependence, the C-terminal transmembrane anchor can partly substitute for this domain. Finally, all Sip proteins were stimulated by added phospholipids, which strongly suggests that phospholipids play an important role in the catalytic mechanism. (C) 2002 Elsevier Science B.V. All rights reserved.
URI: 
ISSN: 0168-1656
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Bacteriology (Rega Institute)
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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