Reconstitution and functional characterization of the FtsH protease in lipid nanodiscs

Prabudiansyah, I.; van der Valk, R.A.; Aubin-Tam, M.E.

doi:10.1016/j.bbamem.2020.183526

Reconstitution and functional characterization of the FtsH protease in lipid nanodiscs

Title

Reconstitution and functional characterization of the FtsH protease in lipid nanodiscs

Author

Prabudiansyah, I. (TU Delft BN/Marie-Eve Aubin-Tam Lab)
van der Valk, R.A. (TU Delft BN/Liedewij Laan Lab)
Aubin-Tam, M.E. (TU Delft BN/Marie-Eve Aubin-Tam Lab)

Date

2021

Abstract

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.

Subject

AAA+ protease
Lipid bilayer
Membrane protein
Nanodisc
Proteolysis

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http://resolver.tudelft.nl/uuid:fa3a2263-fb2f-402d-a4f2-13e73cd2942d

DOI

https://doi.org/10.1016/j.bbamem.2020.183526

ISSN

0005-2736

Source

Biochimica et Biophysica Acta - Biomembranes, 1863 (2)

Part of collection

Institutional Repository