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

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


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 languageEnglish (US)
Pages (from-to)126-136
Number of pages11
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number2
StatePublished - Feb 1 2017

Bibliographical note

Publisher Copyright:
© 2016 Elsevier B.V.


  • Membrane biogenesis
  • Membrane fusion
  • PspA
  • Thylakoid membrane
  • Vipp1


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