A 4: Post-translational modification and enzymatic activity of guanylate-binding proteins
Dr. Gerrit Praefcke
Zentrum für Molekulare Medizin Köln, Universitätsklinikum Köln
email: gpraefck@uni-koeln.de
phone: +49-(0)221 470 1561
website
Running time: 2007 – 2011
Guanylate-binding proteins (GBPs) belong to the dynamin superfamily of large GTPases and show the typical biochemical and functional properties of membrane association, weak nucleotide binding and an assembly stimulated high GTPase activity. We want to investigate the impact of posttranslational modification on the biochemical and cellular functions of GBPs, especially with respect to membrane recruitment and interactions with other proteins. To this end, we want to produce GBPs with C-terminal lipid modifications and conjugated to ubiquitin-like proteins and compare these to the unmodified proteins.
(A final report will follow.)
Publications resulting from the project:
Bade, V., Nickels, J., Keusekotten, K., and Praefcke, G.J.K. (2012). Covalent protein modification with ISG15 via a conserved cysteine in the hinge region. PLoS ONE, Accepted May 8, 2012.
Daumke, O., and Praefcke, G.J.K. (2011). Structural insights into membrane fusion at the endoplasmic reticulum. Proc. Natl. Acad. Sci. U.S.A. 108, 2175-2176.
Anton, F., Fres, J.M., Schauss, A., Pinson, B., Praefcke, G.J.K., Langer, T., and Escobar-Henriques, M. (2011). Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial outer membrane fusion. J. Cell. Sci. J Cell Sci. 124, 1126-1135.
Fres, J.M., Müller, S., and Praefcke, G.J.K. (2010). Purification of the CaaX modified dynamin related large GTPase hGBP1 by co-expression with farnesyltransferase. J. Lipid Res. 51, 2454-2459.