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Interaction of Toposome from Sea-Urchin Yolk Granules with Dimyristoyl Phosphatidylserine Model Membranes: A ²H-NMR Study

Michael Hayley ^*, Jason Emberley , Philip J. Davis ^*, Michael R. Morrow  and John J. Robinson ^*

^* Department of Biochemistry, and Department of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Newfoundland, Canada

Correspondence: Address reprint requests to John J. Robinson, Dept. of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland, A1B 3X9 Canada. Tel.: 709-737-8545; Fax: 709-737-2422; E-mail: johnro{at}mun.ca.

The yolk granule is the most abundant membrane-bound organelle present in sea urchin eggs and embryos. The major protein component of this organelle, toposome, accounts for 50% of the total yolk protein and has been shown to be localized to the embryonic cell surface. Extensive characterization in several laboratories has defined a role for toposome in mediating membrane-membrane interactions. The current study expands the analysis of toposome-membrane interaction by defining toposome-induced changes to the lipid bilayer. The effect of toposome on the biophysical properties of phosphatidyl serine (PS) multibilayers was investigated using deuterium nuclear magnetic resonance and perdeuterated dimyristoyl PS (DMPS-d₅₄). Toposome was found to have little effect on DMPS-d₅₄ chain orientational order in both the gel and liquid-crystalline phases. Timescales for DMPS-d₅₄ reorientation were investigated using quadropole echo decay. Echo decay times were sensitive to toposome in the liquid-crystalline phase but not in the gel phase. Additional information about the perturbation of bilayer motions by toposome was obtained by analyzing its effect on the decay of Carr-Purcell-Meiboom-Gill echo trains. Collectively, these results suggest that toposome interacts peripherally with DMPS bilayers and that it increases the amplitude of lipid reorientation, possibly through local enhancement of bilayer curvature.