The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion

Publication type:
Journal article
Metadata:
Autoren
  • Raoul Hennig
  • Ana West
  • Martina Debus
  • Michael Saur
  • Jürgen Markl
  • Jonathan N Sachs
  • Dirk Schneider
DOI
10.1016/j.bbabio.2016.11.004
ISSN
0005-2728
Ausgabe der Veröffentlichung
2
Zeitschrift
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Sprache
en
Paginierung
126 - 136
Datum der Veröffentlichung
2017
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.bbabio.2016.11.004
Datum der Datenerfassung
2018
Titel
The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion
Ausgabe der Zeitschrift
1858

Data source: Crossref

Other metadata sources:
Abstract
IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contrast, the IM30 C-terminal domain is involved in and necessary to stabilize defined contacts to negatively charged membrane surfaces, and to modulate the IM30-induced membrane fusion activity. Although the two IM30 protein domains have distinct functional roles, only together they enable IM30 to work properly.
Addresses
  • Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, 55128 Mainz, Germany.
Autoren
  • Raoul Hennig
  • Ana West
  • Martina Debus
  • Michael Saur
  • Jürgen Markl
  • Jonathan N Sachs
  • Dirk Schneider
DOI
10.1016/j.bbabio.2016.11.004
eISSN
1879-2650
Externe Identifier
  • PubMed Identifier: 27836697
  • PubMed Central ID: PMC5191951
Funding acknowledgements
  • Max Planck Institutes:
  • University of Mainz:
  • NINDS NIH HHS: R01 NS084998
  • National Institutes of Health: R01 NS084998
Open access
false
ISSN
0005-2728
Ausgabe der Veröffentlichung
2
Zeitschrift
Biochimica et biophysica acta. Bioenergetics
Schlüsselwörter
  • Membranes
  • Chloroplasts
  • Thylakoids
  • Synechocystis
  • Lipid Bilayers
  • Bacterial Proteins
  • Membrane Proteins
  • Membrane Fusion
  • Protein Binding
  • Protein Domains
Sprache
eng
Medium
Print-Electronic
Online publication date
2016
Paginierung
126 - 136
Datum der Veröffentlichung
2017
Status
Published
Datum der Datenerfassung
2016
Titel
The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.
Sub types
  • Research Support, Non-U.S. Gov't
  • research-article
  • Journal Article
  • Research Support, N.I.H., Extramural
Ausgabe der Zeitschrift
1858

Files

https://europepmc.org/articles/PMC5191951?pdf=render

Data source: Europe PubMed Central

Abstract
IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contrast, the IM30 C-terminal domain is involved in and necessary to stabilize defined contacts to negatively charged membrane surfaces, and to modulate the IM30-induced membrane fusion activity. Although the two IM30 protein domains have distinct functional roles, only together they enable IM30 to work properly.
Date of acceptance
2016
Autoren
  • Raoul Hennig
  • Ana West
  • Martina Debus
  • Michael Saur
  • Jürgen Markl
  • Jonathan N Sachs
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/27836697
DOI
10.1016/j.bbabio.2016.11.004
Externe Identifier
  • NIH Manuscript Submission ID: NIHMS828845
  • PubMed Central ID: PMC5191951
Funding acknowledgements
  • NINDS NIH HHS: R01 NS084998
ISSN
0005-2728
Ausgabe der Veröffentlichung
2
Zeitschrift
Biochim Biophys Acta Bioenerg
Schlüsselwörter
  • Membrane biogenesis
  • Membrane fusion
  • PspA
  • Thylakoid membrane
  • Vipp1
  • Bacterial Proteins
  • Chloroplasts
  • Lipid Bilayers
  • Membrane Fusion
  • Membrane Proteins
  • Membranes
  • Protein Binding
  • Protein Domains
  • Synechocystis
  • Thylakoids
Sprache
eng
Country
Netherlands
Paginierung
126 - 136
PII
S0005-2728(16)30656-9
Datum der Veröffentlichung
2017
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2017
Titel
The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.
Sub types
  • Journal Article
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
1858

Data source: PubMed

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