ArticlePloS one2011
Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- HtrA, fatty acids, and membrane protein interplay inJournal of bacteriology · 2024Article
- Repeat infections with chlamydia in women may be more transcriptionally active with lower responses from some immune genes.Frontiers in public health · 2022Article
- Functional analysis and cryo-electron microscopy ofGut microbes · 2020Article
- Article
- Properties of the HtrA Protease From BacteriumFrontiers in microbiology · 2019Article
- Chlamydia Serine Protease Inhibitor, targeting HtrA, as a New Treatment for Koala Chlamydia infection.Scientific reports · 2016Article
- Insights into the Cyanobacterial Deg/HtrA Proteases.Frontiers in plant science · 2016Article
- Article
- A Chlamydia trachomatis strain with a chemically generated amino acid substitution (P370L) in the cthtrA gene shows reduced elementary body production.BMC microbiology · 2015Article
- Proteolytic activation of Chlamydia trachomatis HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5.Cellular & molecular biology letters · 2013Article
- Recombinant outer membrane vesicles carrying Chlamydia muridarum HtrA induce antibodies that neutralize chlamydial infection in vitro.Journal of extracellular vesicles · 2013Article
- The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DegP, a member of the HtrA family of proteins, conducts critical bacterial protein quality control by both chaperone and proteolysis activities. The regulatory mechanisms controlling these two distinct activities, however, are unknown. DegP activation is known to involve a unique mechanism of allosteric binding, conformational changes and oligomer formation. We have uncovered a novel role for the residues at the PDZ1:protease interface in oligomer formation specifically for chaperone substrates of Chlamydia trachomatis HtrA (DegP homolog). We have demonstrated that CtHtrA proteolysis could be activated by allosteric binding and oligomer formation. The PDZ1 activator cleft was required for the activation and oligomer formation. However, unique to CtHtrA was the critical role for residues at the PDZ1:protease interface in oligomer formation when the activator was an in vitro chaperone substrate. Furthermore, a potential in vivo chaperone substrate, the major outer membrane protein (MOMP) from Chlamydia, was able to activate CtHtrA and induce oligomer formation. Therefore, we have revealed novel residues involved in the activation of CtHtrA which are likely to have important in vivo implications for outer membrane protein assembly.
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