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Protein Science, Vol 7, Issue 4 1052-1056, Copyright © 1998 by Cold Spring Harbor Laboratory Press
FOR THE RECORD |
B. BROSIG and D. LANGOSCH
Universitat Heidelberg, Neurobiologie Department, Im Neuenheimer Feld 364, 69120 Heidelberg, Germany
The glycophorin A transmembrane segment homodimerizes to a right-handed pair of {alpha}-helices. Here, we identified the amino acid motif mediating this interaction within a natural membrane environment. Critical residues were grafted onto two different hydrophobic host sequences in a stepwise manner and self-assembly of the hybrid sequences was determined with the ToxR transcription activator system. Our results show that the motif LIxxGxxxGxxxT elicits a level of self-association equivalent to that of the original glycophorin A transmembrane segment. This motif is very similar to the one previously established in detergent solution. Interestingly, the central GxxxG motif by itself already induced strong self-assembly of host sequences and the three-residue spacing between both glycines proved to be optimal for the interaction. The GxxxG element thus appears to be the most crucial part of the interaction motif.
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