אסיף מאגר המחקר החקלאי

Isolation of fusion proteins containing SecY and SecE, components of the protein translocation complex from the halophilic archaeon Haloferax volcanii

Year:

2003

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Volume :

7

Co-Authors:

Irihimovitch, V., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Ring, G., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Elkayam, T., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Konrad, Z., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel
Eichler, J., Department of Life Sciences, Ben Gurion University of the Negev, PO Box 653, Beersheva 84105, Israel

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Abstract:

By exploiting the salt-insensitive interaction of the cellulose-binding domain (CBD) of the Clostridium thermocellum cellulosome with cellulose, purification of CBD-fused versions of SecY and SecE, components of the translocation apparatus of the halophilic archaeon Haloferax volcanii, was undertaken. Following transformation of Haloferax volcanii cells with CBD-SecY- or -SecE-encoding plasmids, cellulose-based purification led to the capture of stably expressed, membrane-bound 68 and 25 kDa proteins, respectively. Both fusion proteins were recognized by antibodies raised against the CBD. Thus, CBD-cellulose interactions can be employed as a salt-insensitive affinity purification system for the capture of complexes containing the Haloferax volcanii translocation apparatus components SecY and SecE. © Springer-Verlag 2002.

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