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