Reconstitution and functional characterization of the FtsH protease in lipid nanodiscs

Irfan Prabudiansyah, Ramon van der Valk, Marie Eve Aubin-Tam*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

2 Citations (Scopus)
50 Downloads (Pure)


FtsH is a membrane-bound protease that plays a crucial role in proteolytic regulation of many cellular functions. It is universally conserved in bacteria and responsible for the degradation of misfolded or misassembled proteins. A recent study has determined the structure of bacterial FtsH in detergent micelles. To properly study the function of FtsH in a native-like environment, we reconstituted the FtsH complex into lipid nanodiscs. We found that FtsH in membrane scaffold protein (MSP) nanodiscs maintains its native hexameric conformation and is functionally active. We further investigated the effect of the lipid bilayer composition (acyl chain length, saturation, head group charge and size) on FtsH proteolytic activity. We found that the lipid acyl chain length influences AaFtsH activity in nanodiscs, with the greatest activity in a bilayer of di-C18:1 PC. We conclude that MSP nanodiscs are suitable model membranes for further in vitro studies of the FtsH protease complex.

Original languageEnglish
Article number183526
Number of pages6
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number2
Publication statusPublished - 2021


  • AAA+ protease
  • Lipid bilayer
  • Membrane protein
  • Nanodisc
  • Proteolysis


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