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J Biol Chem, Vol. 274, Issue 14, 9265-9270, April 2, 1999
From the Universität Heidelberg, Neurobiology Department, Im
Neuenheimer Feld 364, 69120 Heidelberg, Germany
Specific interactions between 
-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.
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