期刊
STRUCTURE
卷 25, 期 9, 页码 1380-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.07.001
关键词
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资金
- Max-Planck graduate center at the Max Planck institutes
- University of Mainz
- Collaborative Research Center of the German Research Foundation (DFG) [SFB 807]
- Cluster of Excellence Frankfurt (Macromolecular Complexes)
- European Research Council under the European Union [337567]
- European Research Council (ERC) [337567] Funding Source: European Research Council (ERC)
Biogenesis and dynamics of thylakoid membranes likely involves membrane fusion events. Membrane attachment of the inner membrane-associated protein of 30 kDa (IM30) affects the structure of the lipid bilayer, finally resulting in membrane fusion. Yet, how IM30 triggers membrane fusion is largely unclear. IM30 monomers pre-assemble into stable tetrameric building blocks, which further align to form oligomeric ring structures, and differently sized IM30 rings bind to membranes. Based on a 3D reconstruction of IM30 rings, we locate the IM30 loop 2 region at the bottom of the ring and show intact membrane binding but missing fusogenic activity of loop 2 mutants. However, helix 7, which has recently been shown to mediate membrane binding, was located at the oppossite, top side of IM30 rings. We propose that a two-sided IM30 ring complex connects two opposing membranes, finally resulting in membrane fusion. Thus, IM30-mediated membrane fusion requires a Janus-faced IM30 ring.
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