ArticleThe Journal of biological chemistry2012
A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 84 citations in OpenAlex.
- The zinc metalloprotease ZMPSTE24 binds a distinct topological isoform of the tail-anchored protein IFITM3.The Journal of biological chemistry · 2026Article
- An In Vitro Assay For LpxC Degradation By The Membrane-Bound Protease FtsH And Adaptor LapB From Escherichia coli.Journal of visualized experiments : JoVE · 2026Article
- Deep Learning-Based Protein Half-Life Prediction for Identifying Rate-Limiting Enzymes in Metabolic Pathways to Alleviate Bottleneck Reactions.Journal of microbiology and biotechnology · 2026Article
- Global analysis of protein degradation reveals instability of diverse regulators inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- The zinc metalloprotease ZMPSTE24 binds a distinct topological isoform of the tail-anchored protein IFITM3.bioRxiv : the preprint server for biology · 2026Article
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.The EMBO journal · 2025Article
- RcsF-independent mechanisms of signaling within the Rcs phosphorelay.PLoS genetics · 2024Article
- RcsF-independent mechanisms of signaling within the Rcs Phosphorelay.bioRxiv : the preprint server for biology · 2024Article
- An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.bioRxiv : the preprint server for biology · 2024Article
- Global protein turnover quantification in Escherichia coli reveals cytoplasmic recycling under nitrogen limitation.Nature communications · 2024Article
- Toxin-based screening of C-terminal tags inbioRxiv : the preprint server for biology · 2024Article
- FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron.Molecular microbiology · 2023Article
- Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli.Nature communications · 2022Article
- Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease inMolecules (Basel, Switzerland) · 2022Article
- Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state.Communications biology · 2022Article
- The protease SPRTN and SUMOylation coordinate DNA-protein crosslink repair to prevent genome instability.Cell reports · 2021Article
- The mitochondrial AAA protease FTSH3 regulates Complex I abundance by promoting its disassembly.Plant physiology · 2021Article
- Article
- Engineering caspase 7 as an affinity reagent to capture proteolytic products.The FEBS journal · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolysis is a universal strategy to rapidly adjust the amount of regulatory and metabolic proteins to cellular demand. FtsH is the only membrane-anchored and essential ATP-dependent protease in Escherichia coli. Among the known functions of FtsH are the control of the heat shock response by proteolysis of the transcription factor RpoH (σ(32)) and its essential role in lipopolysaccharide biosynthesis by degradation of the two key enzymes LpxC and KdtA. Here, we identified new FtsH substrates by using a proteomic-based substrate trapping approach. An FtsH variant (FtsH(trap)) carrying a single amino acid exchange in the proteolytic center was expressed and purified in E. coli. FtsH(trap) is devoid of its proteolytic activity but fully retains ATPase activity allowing for unfolding and translocation of substrates into the inactivated proteolytic chamber. Proteins associated with FtsH(trap) and wild-type FtsH (FtsH(WT)) were purified, separated by two-dimensional PAGE, and subjected to mass spectrometry. Over-representation of LpxC in the FtsH(trap) preparation validated the trapping strategy. Four novel FtsH substrates were identified. The sulfur delivery protein IscS and the d-amino acid dehydrogenase DadA were degraded under all tested conditions. The formate dehydrogenase subunit FdoH and the yet uncharacterized YfgM protein were subject to growth condition-dependent regulated proteolysis. Several lines of evidence suggest that YfgM serves as negative regulator of the RcsB-dependent stress response pathway, which must be degraded under stress conditions. The proteins captured by FtsH(trap) revealed previously unknown biological functions of the physiologically most important AAA(+) protease in E. coli.
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