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Updated: Aug 25, 2026

Recombinant Production And Purification of Hydrophobin SC16 From Escherichia coli And Monitoring of Its Self-Assembly Using Fluorescence Assays
Published on: June 5, 2026
FtsH exists as an exceptionally large complex containing HflKC in the plasma membrane of Escherichia coli
Naoya Saikawa1, Yoshinori Akiyama, Koreaki Ito
1Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.
Abstract:
FtsH is an ATP-dependent and membrane-associated protease, which exerts processive proteolysis against membrane-embedded and soluble substrate proteins. Although previous studies suggested that it functions as a homo-oligomer and it also interacts with HflK-HflC membrane protein complex (HflKC), it is still important to address the question of what kind of supramolecular assembly FtsH forms in wild-type cells. Now we show that FtsH in wild-type Escherichia coli cells exists exclusively as a large complex, termed FtsH holo-enzyme, which can be separated from bulk of membrane proteins after detergent solubilization and velocity sedimentation. This complex appears to have molecular mass of around 1000 kDa. A tentative model is presented that it is composed of hexamers of FtsH and of HflKC, with an ability to bind one or a few substrate molecules.
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