EconPapers    
Economics at your fingertips  
 

IM30 triggers membrane fusion in cyanobacteria and chloroplasts

Raoul Hennig, Jennifer Heidrich, Michael Saur, Lars Schmüser, Steven J. Roeters, Nadja Hellmann, Sander Woutersen, Mischa Bonn, Tobias Weidner, Jürgen Markl and Dirk Schneider ()
Additional contact information
Raoul Hennig: Institut für Pharmazie and Biochemie, Johannes Gutenberg-Universität Mainz
Jennifer Heidrich: Institut für Pharmazie and Biochemie, Johannes Gutenberg-Universität Mainz
Michael Saur: Institut für Zoologie, Johannes Gutenberg-Universität Mainz
Lars Schmüser: Max Planck-Institut für Polymerforschung
Steven J. Roeters: Vant Hoff Institute for Molecular Sciences, University of Amsterdam
Nadja Hellmann: Institut für Molekulare Biophysik, Johannes Gutenberg-Universität Mainz
Sander Woutersen: Vant Hoff Institute for Molecular Sciences, University of Amsterdam
Mischa Bonn: Max Planck-Institut für Polymerforschung
Tobias Weidner: Max Planck-Institut für Polymerforschung
Jürgen Markl: Institut für Zoologie, Johannes Gutenberg-Universität Mainz
Dirk Schneider: Institut für Pharmazie and Biochemie, Johannes Gutenberg-Universität Mainz

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract 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.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms8018 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8018

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8018

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().

 
Page updated 2025-03-19
Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8018