ArticleThe Journal of biological chemistry2011
Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 63 citations in OpenAlex.
- Streptococcus pneumoniae HtrA is a dynamic and monomeric virulence factor capable of forming larger oligomeric complexes.Protein science : a publication of the Protein Society · 2026Article
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Pseudomonas environmental strain produces a DegQ-derived and PDZ domain containing peptide with protease activity.Antonie van Leeuwenhoek · 2024Article
- HtrAs are essential for the survival of the haloarchaeonApplied and environmental microbiology · 2024Article
- In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution.Nature chemical biology · 2023Article
- A Single Residue within the MCR-1 Protein Confers Anticipatory Resilience.Microbiology spectrum · 2023Article
- 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
- 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
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- Development of Resistance inAntibiotics (Basel, Switzerland) · 2020Article
- The unique trimeric assembly of the virulence factor HtrA fromThe Journal of biological chemistry · 2019Article
- Exploring the Potential Role of Moonlighting Function of the Surface-Associated Proteins FromFrontiers in immunology · 2019Article
- Amino-Terminal Processing ofFrontiers in microbiology · 2018Article
- Cryo-EM structure of Nma111p, a unique HtrA protease composed of two protease domains and four PDZ domains.Cell research · 2017Article
- Fast H-DROP: A thirty times accelerated version of H-DROP for interactive SVM-based prediction of helical domain linkers.Journal of computer-aided molecular design · 2017Article
- Release of an HtrA-Like Protease from the Cell Surface of ThermophilicFrontiers in microbiology · 2017Article
- Protein folding in the cell envelope of Escherichia coli.Nature microbiology · 2016Review
- Insights into the Cyanobacterial Deg/HtrA Proteases.Frontiers in plant science · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
To react to distinct stress situations and to prevent the accumulation of misfolded proteins, all cells employ a number of proteases and chaperones, which together set up an efficient protein quality control system. The functionality of proteins in the cell envelope of Escherichia coli is monitored by the HtrA proteases DegS, DegP, and DegQ. In contrast with DegP and DegS, the structure and function of DegQ has not been addressed in detail. Here, we show that substrate binding triggers the conversion of the resting DegQ hexamer into catalytically active 12- and 24-mers. Interestingly, substrate-induced oligomer reassembly and protease activation depends on the first PDZ domain but not on the second. Therefore, the regulatory mechanism originally identified in DegP should be a common feature of HtrA proteases, most of which encompass only a single PDZ domain. Using a DegQ mutant lacking the second PDZ domain, we determined the high resolution crystal structure of a dodecameric HtrA complex. The nearly identical domain orientation of protease and PDZ domains within 12- and 24-meric HtrA complexes reveals a conserved PDZ1 → L3 → LD/L1/L2 signaling cascade, in which loop L3 senses the repositioned PDZ1 domain of higher order, substrate-engaged particles and activates protease function. Furthermore, our in vitro and in vivo data imply a pH-related function of DegQ in the bacterial cell envelope.
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Registered trials
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.