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Folding, curvature and domain formation are characteristics of many
biological membranes. Yet the mechanisms that drive both curvature and the
formation of specialized domains enriched in particular protein complexes are
unknown. For this reason, studies in membranes whose shape and organization are
known under physiological conditions are of great value. We therefore conducted
atomic force microscopy and polarized spectroscopy experiments on membranes of
the photosynthetic bacterium Rhodobacter (Rb.) sphaeroides. These membranes are
densely populated with peripheral light harvesting (LH2) complexes, physically and
functionally connected to dimeric reaction center-light harvesting (RC–LH1–PufX)
complexes. Here, we show that even when converting the dimeric RC-LH1-PufX
complex into RC-LH1 monomers by deleting the gene encoding PufX, both the
appearance of protein domains and the associated membrane curvature are retained.
This suggests that a general mechanism may govern membrane organisation and
shape. Monte Carlo simulations of a membrane model accounting for crowding and
protein geometry alone confirm that these features are sufficient to induce domain
formation and membrane curvature. Our results suggest that coexisting ordered and
fluid domains of like proteins can arise solely from asymmetries in protein size and
shape, without the need to invoke specific interactions. Functionally, coexisting
domains of different fluidity are of enormous importance to allow for diffusive
processes to occur in crowded conditions
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