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Journal of Bacteriology, August 2001, p. 4752-4760, Vol. 183, No. 16
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.16.4752-4760.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Membrane Topology of the Streptomyces lividans Type I Signal Peptidases

Nick Geukens,1 Elke Lammertyn,1 Lieve Van Mellaert,1 Sabine Schacht,1 Kristien Schaerlaekens,1 Victor Parro,2,dagger Sierd Bron,3 Yves Engelborghs,4 Rafael P. Mellado,2 and Jozef Anné1,*

Laboratory of Bacteriology, Rega Institute, Katholieke Universiteit Leuven, 3000 Leuven,1 and Laboratory of Molecular Dynamics, Katholieke Universiteit Leuven, 3001 Heverlee,4 Belgium; Centro Nacional de Biotecnologia (CSIC), Campus de la Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain2; and Department of Genetics, Groningen, Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands3

Received 26 July 2000/Accepted 26 May 2001

Most bacterial membranes contain one or two type I signal peptidases (SPases) for the removal of signal peptides from export proteins. For Streptomyces lividans, four different type I SPases (denoted SipW, SipX, SipY, and SipZ) were previously described. In this communication, we report the experimental determination of the membrane topology of these SPases. A protease protection assay of SPase tendamistat fusions confirmed the presence of the N- as well as the C-terminal transmembrane anchor for SipY. SipX and SipZ have a predicted topology similar to that of SipY. These three S. lividans SPases are currently the only known prokaryotic-type type I SPases of gram-positive bacteria with a C-terminal transmembrane anchor, thereby establishing a new subclass of type I SPases. In contrast, S. lividans SipW contains only the N-terminal transmembrane segment, similar to most type I SPases of gram-positive bacteria. Functional analysis showed that the C-terminal transmembrane anchor of SipY is important to enhance the processing activity, both in vitro as well as in vivo. Moreover, for the S. lividans SPases, a relation seems to exist between the presence or absence of the C-terminal anchor and the relative contributions to the total SPase processing activity in the cell. SipY and SipZ, two SPases with a C-terminal anchor, were shown to be of major importance to the cell. Accordingly, for SipW, missing the C-terminal anchor, a minor role in preprotein processing was found.

* Corresponding author. Mailing address: Laboratory of Bacteriology, Rega Instituut, Katholieke Universiteit Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium. Phone: 32 16 33 73 71. Fax: 32 16 33 73 40. E-mail: Jozef.anne{at}rega.kuleuven.ac.be.

dagger Present address: Centro de Astrobiologia (CSIC-INTA), Torrejón de Ardoz, 28850 Madrid, Spain.

Journal of Bacteriology, August 2001, p. 4752-4760, Vol. 183, No. 16
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.16.4752-4760.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.