IM30 triggers membrane fusion in cyanobacteria and chloroplasts

Publication type:
Journal article
Metadata:
Autoren
  • Raoul Hennig
  • Jennifer Heidrich
  • Michael Saur
  • Lars Schmüser
  • Steven J Roeters
  • Nadja Hellmann
  • Sander Woutersen
  • Mischa Bonn
  • Tobias Weidner
  • Jürgen Markl
  • Dirk Schneider
Sammlungen
  • metadata
ISSN
2041-1723
Zeitschrift
Nature communications
Schlüsselwörter
  • 500 Naturwissenschaften
  • 500 Natural sciences and mathematics
Sprache
eng
Paginierung
Art. 7018
Datum der Veröffentlichung
2015
Herausgeber
Nature Publishing Group
Herausgeber URL
http://dx.doi.org/10.1038/ncomms8018
Datum der Datenerfassung
2020
Datum, an dem der Datensatz öffentlich gemacht wurde
2020
Zugang
Public
Titel
IM30 triggers membrane fusion in cyanobacteria and chloroplasts
Ausgabe der Zeitschrift
6

Data source: METADATA.UB

Other metadata sources:
Autoren
  • Raoul Hennig
  • Jennifer Heidrich
  • Michael Saur
  • Lars Schmüser
  • Steven J Roeters
  • Nadja Hellmann
  • Sander Woutersen
  • Mischa Bonn
  • Tobias Weidner
  • Jürgen Markl
  • Dirk Schneider
DOI
10.1038/ncomms8018
eISSN
2041-1723
Ausgabe der Veröffentlichung
1
Zeitschrift
Nature Communications
Sprache
en
Artikelnummer
7018
Online publication date
2015
Status
Published online
Herausgeber
Springer Science and Business Media LLC
Herausgeber URL
http://dx.doi.org/10.1038/ncomms8018
Datum der Datenerfassung
2023
Titel
IM30 triggers membrane fusion in cyanobacteria and chloroplasts
Ausgabe der Zeitschrift
6

Data source: Crossref

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 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.
Addresses
  • Institut für Pharmazie and Biochemie, Johannes Gutenberg-Universität Mainz, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany.
Autoren
  • Raoul Hennig
  • Jennifer Heidrich
  • Michael Saur
  • Lars Schmüser
  • Steven J Roeters
  • Nadja Hellmann
  • Sander Woutersen
  • Mischa Bonn
  • Tobias Weidner
  • Jürgen Markl
  • Dirk Schneider
DOI
10.1038/ncomms8018
eISSN
2041-1723
Externe Identifier
  • PubMed Identifier: 25952141
Open access
false
ISSN
2041-1723
Zeitschrift
Nature communications
Schlüsselwörter
  • Chloroplasts
  • Thylakoids
  • Synechocystis
  • Glycolipids
  • Galactolipids
  • Phosphatidylglycerols
  • Bacterial Proteins
  • Liposomes
  • Centrifugation, Density Gradient
  • Membrane Fusion
  • Protein Binding
Sprache
eng
Medium
Electronic
Online publication date
2015
Paginierung
7018
Datum der Veröffentlichung
2015
Status
Published
Datum der Datenerfassung
2015
Titel
IM30 triggers membrane fusion in cyanobacteria and chloroplasts.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
6

Data source: Europe PubMed Central

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 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.
Date of acceptance
2015
Autoren
  • Raoul Hennig
  • Jennifer Heidrich
  • Michael Saur
  • Lars Schmüser
  • Steven J Roeters
  • Nadja Hellmann
  • Sander Woutersen
  • Mischa Bonn
  • Tobias Weidner
  • Jürgen Markl
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/25952141
DOI
10.1038/ncomms8018
eISSN
2041-1723
Zeitschrift
Nat Commun
Schlüsselwörter
  • Bacterial Proteins
  • Centrifugation, Density Gradient
  • Chloroplasts
  • Galactolipids
  • Glycolipids
  • Liposomes
  • Membrane Fusion
  • Phosphatidylglycerols
  • Protein Binding
  • Synechocystis
  • Thylakoids
Sprache
eng
Country
England
Paginierung
7018
PII
ncomms8018
Datum der Veröffentlichung
2015
Status
Published online
Datum, an dem der Datensatz öffentlich gemacht wurde
2016
Titel
IM30 triggers membrane fusion in cyanobacteria and chloroplasts.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
6

Data source: PubMed

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