6533b7d1fe1ef96bd125d8be

RESEARCH PRODUCT

IM30 triggers membrane fusion in cyanobacteria and chloroplasts

Mischa BonnTobias WeidnerRaoul HennigSteven J. RoetersSander WoutersenJennifer HeidrichJürgen MarklDirk SchneiderNadja HellmannLars SchmüserMichael Saur

subject

ChloroplastsGeneral Physics and AstronomyBiologyMembrane FusionThylakoidsGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsCentrifugation Density GradientIntegral membrane proteinMultidisciplinaryGalactolipidsPeripheral membrane proteinSynechocystisLipid bilayer fusionfood and beveragesPhosphatidylglycerolsGeneral ChemistryTransmembrane proteinCell biologyChloroplastMembraneThylakoidLiposomesQuantasomeGlycolipidsProtein Binding

description

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 Mg2+, 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. Thylakoid membranes are critical components of chloroplasts and cyanobacteria. Here, Hennig et al. demonstrate that IM30, a conserved chloroplast and cyanobacterial protein, binds to thylakoid membranes and can trigger membrane destabilization and fusion in a Mg2+dependent manner.

10.1038/ncomms8018https://doi.org/10.1038/ncomms8018