An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins

ABSTRACT: The AAA-protease FtsH associates with HflK/C subunits to form a megadalton-size complex that spans the inner membrane and extends into the periplasm of E. coli. How this bacterial complex and homologous assemblies in eukaryotic organelles recruit, extract, and degrade membrane-embedded substrates is unclear. Following overproduction of protein components, recent cryo-EM structures showed symmetric HflK/C cages surrounding FtsH in a manner proposed to inhibit degradation of membrane-embedded substrates. Here, we present structures of native protein complexes, in which HflK/C instead forms an asymmetric nautilus-shaped assembly with an entryway for membrane-embedded substrates to reach and be engaged by FtsH. Consistent with this nautilus-like structure, proteomic assays suggest that HflK/C

SUBMITTER: Alireza Ghanbarpour 

PROVIDER: S-SCDT-10_1038-S44318-025-00408-1 | biostudies-other |

REPOSITORIES: biostudies-other