The full-length cell–cell fusogen EFF-1 is monomeric and upright on the membrane

Tzviya Zeev-Ben-Mordehai, Daven Vasishtan, C. Alistair Siebert and Kay Grünewald ()
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Tzviya Zeev-Ben-Mordehai: Oxford Particle Imaging Centre, Wellcome Trust Centre for Human Genetics, University of Oxford
Daven Vasishtan: Oxford Particle Imaging Centre, Wellcome Trust Centre for Human Genetics, University of Oxford
C. Alistair Siebert: Oxford Particle Imaging Centre, Wellcome Trust Centre for Human Genetics, University of Oxford
Kay Grünewald: Oxford Particle Imaging Centre, Wellcome Trust Centre for Human Genetics, University of Oxford

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract Fusogens are membrane proteins that remodel lipid bilayers to facilitate membrane merging. Although several fusogen ectodomain structures have been solved, structural information on full-length, natively membrane-anchored fusogens is scarce. Here we present the electron cryo microscopy three-dimensional reconstruction of the Caenorhabditis elegans epithelial fusion failure 1 (EFF-1) protein natively anchored in cell-derived membrane vesicles. This reveals a membrane protruding, asymmetric, elongated monomer. Flexible fitting of a protomer of the EFF-1 crystal structure, which is homologous to viral class-II fusion proteins, shows that EFF-1 has a hairpin monomeric conformation before fusion. These structural insights, when combined with our observations of membrane-merging intermediates between vesicles, enable us to propose a model for EFF-1 mediated fusion. This process, involving identical proteins on both membranes to be fused, follows a mechanism that shares features of SNARE-mediated fusion while using the structural building blocks of the unilaterally acting class-II viral fusion proteins.

Date: 2014
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DOI: 10.1038/ncomms4912

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