Gunnar von Heijne

Table of contents

    Research Project: 

       

    Membrane protein assembly and structure.

            

    Address: 

       

    E-mail: gunnar@dbb.su.se
    Phone: (+46)-8-16 2590
    Fax: (+46)-8-15 3679

            

    Research group

       

    Andreas Bernsel, Joy Kim, Roger Draheim, Joanna Slusky, Morten Nørholm, Susanna Seppälä, Marie Österberg, Salomé Botelho, Karin Geiger, Pilar Lloris.

            

    Project description

        

    Membrane proteins serve a number of very important functions in both prokaryotic and eukaryotic cells. They are built according to structural principles different from those of globular proteins. A full understanding of membrane proteins requires a conceptual framework where processes of protein translocation across membranes and the physical chemistry of lipid-protein interactions play major roles.

        

    We have a long-standing interest in problems related to membrane protein assembly and structure. Work in our lab has pointed to the central importance of positively charged amino acids as determinants of membrane protein topology, has led to the development of new theoretical methods for predicting transmembrane segments, and has illuminated many aspects of membrane protein assembly in both prokaryotic and eukaryotic cells. Ongoing theoretical and experimental work is directed towards both the topology and 3D structure of membrane proteins.


    Recent papers

    Lundin, C., Kim, H., Nilsson, IM., White, S.H., and von Heijne, G. (2008) The molecular code for protein insertion in the ER membrane is similar for Nin-Cout and Nout-Cin transmembrane helices. Proc.Natl.Acad.Sci. USA, in press.

         

    Bernsel, A., Viklund, H., Falk, J., Lindahl, E., von Heijne, G., and Elofsson, A. (2008) Prediction of membrane-protein topology from first principles. Proc.Natl.Acad.Sci. USA 105, 7177-7181.

         

    Hessa, T., Meindl-Beinker, N.M., Bernsel, A., Kim, H., Sato, Y., Lerch-Bader, M., Nilsson, IM., White, S.H., and von Heijne, G. (2007) The molecular code for transmembrane-helix recognition by the ER translocon. Nature 450, 1026-1030. 

         

    Rapp, M., Seppälä, S., Granseth, E., and von Heijne, G. (2007) Emulating membrane protein evolution by rational design. Science 315, 1282-1284.

         

    Rapp, M., Seppälä, S., Granseth, E., and von Heijne, G. (2006) Identification and evolution of dual topology membrane proteins. Nature Struct.Mol.Biol. 13, 112-116.

         

    Kim, H., Melén, K., Österberg, M., and von Heijne, G. (2006) A global topology map of  the Saccharomyces cerevisiae membrane proteome. Proc.Natl.Acad.Sci. USA 103, 11142- 11147

         

    Daley, D.O., Rapp, M., Granseth, E., Melén, K., Drew, D., and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308, 1321-1323.

         

    Hessa, T., Kim., H., Bihlmaier, K., Lundin, C., Boekel, J., Andersson, H., Nilsson, I.M., White, S.H., and von Heijne, G. (2005) Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433, 377-381.

         

    Hessa, T., White, S.H., and von Heijne, G. (2005) Membrane insertion of a potassium channel voltage sensor. Science 307, 1427.

         

    Drew, D., Sjöstrand, D., Nilsson, J., Urbig, T., Chin, C., de Gier, J-W., and von Heijne, G. (2002) Rapid topology mapping of E. coli inner membrane proteins by prediction and PhoA/GFP fusion analysis. Proc.Natl.Acad.Sci.USA 99, 2690-2695.
     

    Full publication list, see http://www.sbc.su.se/gunnar/gvhpub.html


    Acknowledgments

      

    The group is supported by grants from the Swedish Research Council, the Swedish Cancer Foundation, the Foundation for Strategic Research, the European Community, the Human Frontiers Science Program, and the National Institutes of Health.

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