ArticleThe Journal of biological chemistry
The cytoplasmic domain of the AAA+ protease FtsH is tilted with respect to the membrane to facilitate substrate entry.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Cryo-EM Structure of the FtsH Periplasmic Domain Reveals Functional Dynamics.ACS chemical biology · 2026Article
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- Off-target structural insights: ArnA and AcrB in bacterial membrane-protein cryo-EM analysis.Acta crystallographica. Section D, Structural biology · 2025Article
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- Signaling through theJournal of bacteriology · 2024Article
- Investigation of CRISPR-Independent Phage Resistance Mechanisms Reveals a Role for FtsH in Phage Adsorption to Streptococcus thermophilus.Journal of bacteriology · 2023Article
- Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria.Microbial cell (Graz, Austria) · 2022Review
- FtsH degrades dihydrofolate reductase by recognizing a partially folded species.Protein science : a publication of the Protein Society · 2022Article
- Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state.Communications biology · 2022Article
- Recent Advances in Understanding the Structural and Functional Evolution of FtsH Proteases.Frontiers in plant science · 2022Review
- Characterization of FtsH Essentiality inFrontiers in genetics · 2021Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AAA+ proteases are degradation machines that use ATP hydrolysis to unfold protein substrates and translocate them through a central pore toward a degradation chamber. FtsH, a bacterial membrane-anchored AAA+ protease, plays a vital role in membrane protein quality control. How substrates reach the FtsH central pore is an open key question that is not resolved by the available atomic structures of cytoplasmic and periplasmic domains. In this work, we used both negative stain TEM and cryo-EM to determine 3D maps of the full-length Aquifex aeolicus FtsH protease. Unexpectedly, we observed that detergent solubilization induces the formation of fully active FtsH dodecamers, which consist of two FtsH hexamers in a single detergent micelle. The striking tilted conformation of the cytosolic domain in the FtsH dodecamer visualized by negative stain TEM suggests a lateral substrate entrance between the membrane and cytosolic domain. Such a substrate path was then resolved in the cryo-EM structure of the FtsH hexamer. By mapping the available structural information and structure predictions for the transmembrane helices to the amino acid sequence we identified a linker of ∼20 residues between the second transmembrane helix and the cytosolic domain. This unique polypeptide appears to be highly flexible and turned out to be essential for proper functioning of FtsH as its deletion fully eliminated the proteolytic activity of FtsH.
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