ArticleProceedings of the National Academy of Sciences of the United States of America2012
Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 59 citations in OpenAlex.
- MucD regulates alginate biosynthesis through the proteolytic control of AlgX and AlgK in Pseudomonas aeruginosa.PLoS biology · 2026Article
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- YdbL directly modulates YdbH-YnbE bridge formation to maintainbioRxiv : the preprint server for biology · 2026Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Function, molecular mechanisms, and therapeutic potential of bacterial HtrA proteins: An evolving view.Computational and structural biotechnology journal · 2022Review
- Structural basis of DegP protease temperature-dependent activation.Science advances · 2021Article
- Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Gene-specific mutagenesis enables rapid continuous evolution of enzymes in vivo.Nucleic acids research · 2021Article
- Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The proteolytic activity of Listeria monocytogenes HtrA.BMC microbiology · 2019Article
- The unique trimeric assembly of the virulence factor HtrA fromThe Journal of biological chemistry · 2019Article
- The Role of Proteases in the Virulence of Plant Pathogenic Bacteria.International journal of molecular sciences · 2019Review
- Properties of the HtrA Protease From BacteriumFrontiers in microbiology · 2019Article
- Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation.Molecules (Basel, Switzerland) · 2018Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Regulation of Proteolysis in the Gram-Negative Bacterial Envelope.Journal of bacteriology · 2018Article
- A Small Periplasmic Protein with a Hydrophobic C-Terminal Residue Enhances DegP Proteolysis as a Suicide Activator.Journal of bacteriology · 2018Article
- HtrA1 activation is driven by an allosteric mechanism of inter-monomer communication.Scientific reports · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
DegP, a member of the highly conserved HtrA family, performs quality-control degradation of misfolded proteins in the periplasm of gram-negative bacteria and is required for high-temperature survival of Escherichia coli. Substrate binding transforms DegP from an inactive oligomer containing two trimers into active polyhedral cages, typically containing four or eight trimers. Although these observations suggest a causal connection, we show that cage assembly and proteolytic activation can be uncoupled. Indeed, DegP variants that remain trimeric, hexameric, or dodecameric in the presence or absence of substrate still display robust and positively cooperative substrate degradation in vitro and, most importantly, sustain high-temperature bacterial growth as well as the wild-type enzyme. Our results support a model in which substrate binding converts inactive trimers into proteolytically active trimers, and simultaneously leads to cage assembly by enhancing binding of PDZ1 domains in one trimer to PDZ2' domains in neighboring trimers. Thus, both processes depend on substrate binding, but they can be uncoupled without loss of biological function. We discuss potential coupling mechanisms and why cage formation may have evolved if it is not required for DegP proteolysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.