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Biophys J, November 2000, p. 2624-2631, Vol. 79, No. 5

PMP1 18-38, A Yeast Plasma Membrane Protein Fragment, Binds Phosphatidylserine from Bilayer Mixtures with Phosphatidylcholine: A 2H-NMR Study

Michel Roux,* Veronica Beswick,dagger Yves-Marie Coïc,Dagger Tam Huynh-Dinh,Dagger Alain Sanson,*§ and Jean-Michel Neumann*

 *Département de Biologie Cellulaire et Moléculaire, Section de Biophysique des Protéines et des Membranes, CEA and URA CNRS 2096, Centre d'Etudes de Saclay, 91191 Gif sur Yvette Cedex, France;  dagger Université d'Evry-Val d'Essonne, 91025 Evry Cedex, France;  Dagger Unité de Chimie Organique, URA CNRS 487, Institut Pasteur, 75724 Paris Cedex 15, France; and  §Université Pierre et Marie Curie, 75005 Paris, France

PMP1 is a 38-residue plasma membrane protein of the yeast Saccharomyces cerevisiae that regulates the activity of the H+-ATPase. The cytoplasmic domain conformation results in a specific interfacial distribution of five basic side chains, thought to strongly interact with anionic phospholipids. We have used the PMP1 18-38 fragment to carry out a deuterium nuclear magnetic resonance (2H-NMR) study for investigating the interactions between the PMP1 cytoplasmic domain and phosphatidylserines. For this purpose, mixed bilayers of 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphoserine (POPS) were used as model membranes (POPC/POPS 5:1, m/m). Spectra of headgroup- and chain-deuterated POPC and POPS phospholipids, POPC-d4, POPC-d31, POPS-d3, and POPS-d31, were recorded at different temperatures and for various concentrations of the PMP1 fragment. Data obtained from POPS deuterons revealed the formation of specific peptide-POPS complexes giving rise to a slow exchange between free and bound PS lipids, scarcely observed in solid-state NMR studies of lipid-peptide/protein interactions. The stoichiometry of the complex (8 POPS per peptide) was determined and its significance is discussed. The data obtained with headgroup-deuterated POPC were rationalized with a model that integrates the electrostatic perturbation induced by the cationic peptide on the negatively charged membrane interface, and a "spacer" effect due to the intercalation of POPS/PMP1f complexes between choline headgroups.

Biophys J, November 2000, p. 2624-2631, Vol. 79, No. 5
© 2000 by the Biophysical Society   0006-3495/00/11/2624/08  $2.00


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