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

Raoul Hennig; Ana West; Martina Debus; Michael Saur; Jürgen Markl; Jonathan N. Sachs; Dirk Schneider

doi:10.1016/j.bbabio.2016.11.004

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

Raoul Hennig, Ana West, Martina Debus, Michael Saur, Jürgen Markl, Jonathan N. Sachs, Dirk Schneider

Biomedical Engineering

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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.

Original language	English (US)
Pages (from-to)	126-136
Number of pages	11
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	1858
Issue number	2
DOIs	https://doi.org/10.1016/j.bbabio.2016.11.004
State	Published - Feb 1 2017

Bibliographical note

Funding Information:
This work was funded by the Max-Planck graduate center at the Max Planck Institutes and the University of Mainz (to R.H and D.S.). A.W. and J.N.S. gratefully acknowledge funding from the National Institutes of Health ( R01 NS084998 to J.N.S.). All simulations were conducted using resources of Minnesota Supercomputing Institute ( https://www.msi.umn.edu /).

Publisher Copyright:
© 2016 Elsevier B.V.

Keywords

Membrane biogenesis
Membrane fusion
PspA
Thylakoid membrane
Vipp1

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

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.",

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author = "Raoul Hennig and Ana West and Martina Debus and Michael Saur and J{\"u}rgen Markl and Sachs, {Jonathan N.} and Dirk Schneider",

note = "Funding Information: This work was funded by the Max-Planck graduate center at the Max Planck Institutes and the University of Mainz (to R.H and D.S.). A.W. and J.N.S. gratefully acknowledge funding from the National Institutes of Health ( R01 NS084998 to J.N.S.). All simulations were conducted using resources of Minnesota Supercomputing Institute ( https://www.msi.umn.edu /). Publisher Copyright: {\textcopyright} 2016 Elsevier B.V.",

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AU - Sachs, Jonathan N.

AU - Schneider, Dirk

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N2 - 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.

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

Abstract

Bibliographical note

Keywords

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