ArticleProceedings of the National Academy of Sciences of the United States of America2011
The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Application of biophysical methods for improved protein production and characterization: A case study on an high-temperature requirement A-family bacterial protease.Protein science : a publication of the Protein Society · 2022Article
- Legionella pneumophila Cas2 Promotes the Expression of Small Heat Shock Protein C2 That Is Required for Thermal Tolerance and Optimal Intracellular Infection.Infection and immunity · 2022Article
- The Tail-Specific Protease Is Important for Legionella pneumophila To Survive Thermal Stress in Water and inside Amoebae.Applied and environmental microbiology · 2021Article
- Article
- Functional analysis and cryo-electron microscopy ofGut microbes · 2020Article
- The proteolytic activity of Listeria monocytogenes HtrA.BMC microbiology · 2019Article
- Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.Cell death & disease · 2017Article
- HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogens.Cell communication and signaling : CCS · 2016Article
- Magnetite Biomineralization in Magnetospirillum magneticum Is Regulated by a Switch-like Behavior in the HtrA Protease MamE.The Journal of biological chemistry · 2016Article
- HtrA Is Important for Stress Resistance and Virulence in Haemophilus parasuis.Infection and immunity · 2016Article
- MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria.PLoS biology · 2016Article
- Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants.PloS one · 2016Article
- Insights into the Cyanobacterial Deg/HtrA Proteases.Frontiers in plant science · 2016Article
- Structural basis of the proteolytic and chaperone activity of Chlamydia trachomatis CT441.Journal of bacteriology · 2015Article
- Article
- Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.Cellular and molecular life sciences : CMLS · 2013Review
- Article
- The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.The Journal of biological chemistry · 2012Article
- Crystal structure of Arabidopsis Deg2 protein reveals an internal PDZ ligand locking the hexameric resting state.The Journal of biological chemistry · 2012Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases of the HtrA family are key factors dealing with folding stress in the periplasmatic compartment of prokaryotes. In Escherichia coli, the well-characterized HtrA family members DegS and DegP counteract the accumulation of unfolded outer-membrane proteins under stress conditions. Whereas DegS serves as a folding-stress sensor, DegP is a chaperone-protease facilitating refolding or degradation of defective outer-membrane proteins. Here, we report the 2.15-Å-resolution crystal structure of the second major chaperone-protease of the periplasm, DegQ from Legionella fallonii. DegQ assembles into large, cage-like 12-mers that form independently of unfolded substrate proteins. We provide evidence that 12-mer formation is essential for the degradation of substrate proteins but not for the chaperone activity of DegQ. In the current model for the regulation of periplasmatic chaperone-proteases, 6-meric assemblies represent important protease-resting states. However, DegQ is unable to form such 6-mers, suggesting divergent regulatory mechanisms for DegQ and DegP. To understand how the protease activity of DegQ is controlled, we probed its functional properties employing designed protein variants. Combining crystallographic, biochemical, and mutagenic data, we present a mechanistic model that suggests how protease activity of DegQ 12-mers is intrinsically regulated and how deleterious proteolysis by free DegQ 3-mers is prevented. Our study sheds light on a previously uncharacterized component of the prokaryotic stress-response system with implications for other members of the HtrA family.
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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.