ArticleScience advances2021
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.
Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Structural Analysis of Human LonP1 Protease Bound with the Native Substrate.Life (Basel, Switzerland) · 2026Article
- Bifurcated assembly pathway and dual function of a Lon-like protease revealed by cryo-EM Analysis.Fundamental research · 2026Article
- Cereblon induces G3BP2 neosubstrate degradation using molecular surface mimicry.Nature structural & molecular biology · 2026Article
- Structures of Helicobacter pylori C-terminal protease CtpA reveal a new mode of self-contained proteolytic processing.Communications biology · 2025Article
- TopEC: prediction of Enzyme Commission classes by 3D graph neural networks and localized 3D protein descriptor.Nature communications · 2025Article
- Structural basis for the allosteric activation of Lon by the heat shock protein LarA.Nature communications · 2025Article
- Elucidating the Architectural dynamics of MuB filaments in bacteriophage Mu DNA transposition.Nature communications · 2024Article
- A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine.Nature communications · 2023Article
- TNFα increases the degradation of pyruvate dehydrogenase kinase 4 by the Lon protease to support proinflammatory genes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism.Biochemical Society transactions · 2023Article
- Enzyme-substrate hybrid β-sheet controls geometry and water access to the γ-secretase active site.Communications biology · 2023Article
- A model industrial workhorse: Bacillus subtilis strain 168 and its genome after a quarter of a century.Microbial biotechnology · 2023Review
- Unique Structural Fold of LonBA Protease fromInternational journal of molecular sciences · 2022Article
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a processive fashion, cutting a protein chain processively into small peptides before commencing cleavages of another protein chain. Here, we present structural and biochemical evidence demonstrating that processive substrate degradation occurs at each of the six proteolytic active sites of Lon, which forms a deep groove that partially encloses the substrate polypeptide chain by accommodating only the unprimed residues and permits processive cleavage in the C-to-N direction. We identify a universally conserved acidic residue at the exit side of the binding groove indispensable for the proteolytic activity. This noncatalytic residue likely promotes processive proteolysis by carboxyl-carboxylate interactions with cleaved intermediates. Together, these results uncover a previously unrecognized mechanism for processive substrate degradation by the Lon protease.
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