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IM30 triggers membrane fusion in cyanobacteria and chloroplasts

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DOI

  • Raoul Hennig, Johannes Gutenberg University Mainz
  • ,
  • Jennifer Heidrich, Johannes Gutenberg University Mainz
  • ,
  • Michael Saur, Johannes Gutenberg University Mainz
  • ,
  • Lars Schmüser, Max Planck-Institut für Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany.
  • ,
  • Steven J Roeters, Vant Hoff Institute for Molecular Sciences, University of Amsterdam, Science Park 904, 1098 XH, Amsterdam, The Netherlands.
  • ,
  • Nadja Hellmann, Johannes Gutenberg University Mainz
  • ,
  • Sander Woutersen, Vant Hoff Institute for Molecular Sciences, University of Amsterdam, Science Park 904, 1098 XH, Amsterdam, The Netherlands.
  • ,
  • Mischa Bonn, Max Planck-Institut für Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany.
  • ,
  • Tobias Weidner
  • Jürgen Markl, Johannes Gutenberg University Mainz
  • ,
  • Dirk Schneider, Johannes Gutenberg University Mainz

The thylakoid membrane of chloroplasts and cyanobacteria is a unique internal membrane system harbouring the complexes of the photosynthetic electron transfer chain. Despite their apparent importance, little is known about the biogenesis and maintenance of thylakoid membranes. Although membrane fusion events are essential for the formation of thylakoid membranes, proteins involved in membrane fusion have yet to be identified in photosynthetic cells or organelles. Here we show that IM30, a conserved chloroplast and cyanobacterial protein of approximately 30 kDa binds as an oligomeric ring in a well-defined geometry specifically to membranes containing anionic lipids. Triggered by Mg(2+), membrane binding causes destabilization and eventually results in membrane fusion. We propose that IM30 establishes contacts between internal membrane sites and promotes fusion to enable regulated exchange of proteins and/or lipids in cyanobacteria and chloroplasts.

Original languageEnglish
JournalNature Communications
Volume6
Issue7018
Pages (from-to)7018
Number of pages10
ISSN2041-1723
DOIs
Publication statusPublished - 2015
Externally publishedYes

    Research areas

  • Bacterial Proteins, Centrifugation, Density Gradient, Chloroplasts, Galactolipids, Glycolipids, Liposomes, Membrane Fusion, Phosphatidylglycerols, Protein Binding, Synechocystis, Thylakoids, Journal Article, Research Support, Non-U.S. Gov't

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