Interaction of toposome from sea-urchin yolk granules with dimyristoyl phosphatidylserine model membranes: a 2H-NMR study.

Abstract:

: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 and perdeuterated dimyristoyl PS (DMPS-d(54)). Toposome was found to have little effect on DMPS-d(54) chain orientational order in both the gel and liquid-crystalline phases. Timescales for DMPS-d(54) 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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Hayley M,Emberley J,Davis PJ,Morrow MR,Robinson JJ

doi

10.1529/biophysj.106.089979

subject

Has Abstract

pub_date

2006-12-15 00:00:00

pages

4555-64

issue

12

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(06)72167-1

journal_volume

91

pub_type

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