Interaction of toposome from sea-urchin yolk granules with dimyristoyl phosphatidylserine model membranes: a 2H-NMR study
Michael J Hayley 1, Jason Emberley 1, Philip J Davis 1, Michael R Morrow 1 and John J Robinson 1*
1 Memorial University
* To whom correspondence should be addressed. E-mail: johnro{at}mun.ca.
Submitted on May 25, 2006
Revised on July 3, 2006
Accepted on 7 September 2006
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Abstract |
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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 approximately 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 (2H-NMR) and perdeuterated dimyristoyl phosphatidylserine (DMPS-d54). Toposome was found to have little effect on DMPS-d54 chain orientational order in both the gel and liquid-crystalline phase. 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 analysing 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.
Key Words:
Calcium, Sea Urchin, Toposome-Membrane Interaction
