Protein Shape and Crowding Drive Domain Formation and Curvature in Biological Membranes


Frese, Raoul N. and Pamies, Josep C. and Olsen, John D. and Bahatyrova, Svetlana and Weij-de Wit, Chantal D. van der and Aartsma, Thijs J. and Otto, Cees and Hunter, C. Neil and Frenkel, Daan and Grondelle, Rienk (2007) Protein Shape and Crowding Drive Domain Formation and Curvature in Biological Membranes. Biophysical Journal, 94 (2). pp. 640-647. ISSN 0006-3495

[img] PDF
Restricted to UT campus only
: Request a copy
Abstract: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 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 organization 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.

Item Type:Article
Copyright:© 2008 The Biophysical Society
Science and Technology (TNW)
Research Group:
Link to this item:
Official URL:
Export this item as:BibTeX
HTML Citation
Reference Manager


Repository Staff Only: item control page

Metis ID: 243363