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J Biol Chem, Vol. 274, Issue 14, 9265-9270, April 2, 1999

A Heptad Motif of Leucine Residues Found in Membrane Proteins Can Drive Self-assembly of Artificial Transmembrane Segments

Rolf Gurezka, Rico Laage, Bettina Brosig, and Dieter Langosch

From the Universität Heidelberg, Neurobiology Department, Im Neuenheimer Feld 364, 69120 Heidelberg, Germany

Specific interactions between alpha -helical transmembrane segments are important for folding and/or oligomerization of membrane proteins. Previously, we have shown that most transmembrane helix-helix interfaces of a set of crystallized membrane proteins are structurally equivalent to soluble leucine zipper interaction domains. To establish a simplified model of these membrane-spanning leucine zippers, we studied the homophilic interactions of artificial transmembrane segments using different experimental approaches. Importantly, an oligoleucine, but not an oligoalanine, se- quence efficiently self-assembled in membranes as well as in detergent solution. Self-assembly was maintained when a leucine zipper type of heptad motif consisting of leucine residues was grafted onto an alanine host sequence. Analysis of point mutants or of a random sequence confirmed that the heptad motif of leucines mediates self-recognition of our artificial transmembrane segments. Further, a data base search identified degenerate versions of this leucine motif within transmembrane segments of a variety of functionally different proteins. For several of these natural transmembrane segments, self-interaction was experimentally verified. These results support various lines of previously reported evidence where these transmembrane segments were implicated in the oligomeric assembly of the corresponding proteins.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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