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TitleAn asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.
Journal, issue, pagesEMBO J, Vol. 44, Issue 9, Page 2501-2513, Year 2025
Publish dateMar 13, 2025
AuthorsAlireza Ghanbarpour / Bertina Telusma / Barrett M Powell / Jia Jia Zhang / Isabella Bolstad / Carolyn Vargas / Sandro Keller / Tania A Baker / Robert T Sauer / Joseph H Davis /
PubMed AbstractThe 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 ...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 the overproduction of protein components, recent cryo-EM structures showed symmetric HflK/C cages surrounding FtsH in a manner proposed to inhibit the 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 enhances FtsH degradation of certain membrane-embedded substrates. Membrane curvature in our FtsH•HflK/C complexes is opposite that of surrounding membrane regions, a property that correlates with lipid scramblase activity and possibly with FtsH's function in the degradation of membrane-embedded proteins.
External linksEMBO J / PubMed:40082723 / PubMed Central
MethodsEM (single particle)
Resolution4.4 - 12.0 Å
Structure data

46057

9cz2

EMDB-46057, PDB-9cz2:
Cryo-EM structure of a nautilus-like HflK/C assembly in complex with FtsH AAA protease
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-46058: Cryo-EM structure of a nautilus-like HflK/C assembly in complex with FtsH AAA protease extracted endogenously from E. coli using DIBMA polymer
Method: EM (single particle) / Resolution: 12.0 Å

EMDB-46059: Cryo-EM structure of the endogenously extracted FtsH.HflK.HflC complex with two FtsH hexamers per nautilus-like HflK.HflC assembly
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-46061: Cryo-EM structure of the endogenously extracted FtsH.HflK.HflC complex with one FtsH hexamer per nautilus-like HflK.HflC assembly
Method: EM (single particle) / Resolution: 6.6 Å

EMDB-46062: Cryo-EM structure of the overexpressed HflK.HflC complex
Method: EM (single particle) / Resolution: 7.7 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli bl21 (bacteria)
KeywordsCHAPERONE / FtsH / HflK / HflC / AAA protease

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