ArticleStructure (London, England : 1993)2015
A conserved activation cluster is required for allosteric communication in HtrA-family proteases.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.Structure (London, England : 1993) · 2026Article
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Fever-like temperature bursts promote competence development via an HtrA-dependent pathway in Streptococcus pneumoniae.PLoS genetics · 2023Article
- Peptidase Activation by a Leader Peptide-Bound RiPP Recognition Element.Biochemistry · 2023Article
- 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
- Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs.Journal of molecular biology · 2022Review
- Properties of the HtrA Protease From BacteriumFrontiers in microbiology · 2019Article
- Solution Structure of SpoIVB Reveals Mechanism of PDZ Domain-Regulated Protease Activity.Frontiers in microbiology · 2019Article
- Structural basis of inactivation of human counterpart of mouse motor neuron degeneration 2 mutant in serine protease HtrA2.Bioscience reports · 2018Article
- Regulation of Proteolysis in the Gram-Negative Bacterial Envelope.Journal of bacteriology · 2018Article
- Amino-Terminal Processing ofFrontiers in microbiology · 2018Article
- HtrA1 activation is driven by an allosteric mechanism of inter-monomer communication.Scientific reports · 2017Article
- Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.Cell death & disease · 2017Article
- ThePeerJ · 2017Article
- Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants.PloS one · 2016Article
- Steric clashes with bound OMP peptides activate the DegS stress-response protease.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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6 authors at 2 institutions in 1 country.
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Abstract
In E. coli, outer-membrane stress causes a transcriptional response through a signaling cascade initiated by DegS cleavage of a transmembrane antisigma factor. Each subunit of DegS, an HtrA-family protease, contains a protease domain and a PDZ domain. The trimeric protease domain is autoinhibited by the unliganded PDZ domains. Allosteric activation requires binding of unassembled outer-membrane proteins (OMPs) to the PDZ domains and protein substrate binding. Here, we identify a set of DegS residues that cluster together at subunit-subunit interfaces in the trimer, link the active sites and substrate binding sites, and are crucial for stabilizing the active enzyme conformation in response to OMP signaling. These residues are conserved across the HtrA-protease family, including orthologs linked to human disease, supporting a common mechanism of allosteric activation. Indeed, mutation of residues at homologous positions in the DegP quality-control protease also eliminates allosteric activation.
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