PMID: 2119256Sep 21, 1990Paper

Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids

Cell
I Nilsson, G von Heijne

Abstract

The effects of positively and negatively charged residues on the membrane topology of a model E. coli protein with two transmembrane segments have been studied. We show that addition or removal of as little as a single positively charged lysine residue in one of two critical regions can be sufficient to reverse the transmembrane topology of the molecule from Nout-Cout to Nin-Cin. Negatively charged residues are much less potent and significantly affect the topology only if present in high numbers. Finally, we provide data to suggest that sec-independent and sec-dependent translocation mechanisms differ in their sensitivity to positively charged amino acids.

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Citations

Aug 1, 1996·Protein Science : a Publication of the Protein Society·B RostR Casadio
May 6, 1998·Protein Science : a Publication of the Protein Society·E Wallin, G von Heijne
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