ArticleThe Journal of biological chemistry2012
Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 56 citations in OpenAlex.
- Review
- An up-to-date review of biomedical applications of serratiopeptidase and its biobetter derivatives as a multi-potential metalloprotease.Archives of microbiology · 2024Review
- Unveiling the Secrets of Calcium-Dependent Proteins in Plant Growth-Promoting Rhizobacteria: An Abundance of Discoveries Awaits.Plants (Basel, Switzerland) · 2023Review
- A serralysin-like protein ofFrontiers in microbiology · 2022Article
- Design, expression and functional assessment of novel engineered serratiopeptidase analogs with enhanced protease activity and thermal stability.World journal of microbiology & biotechnology · 2021Article
- PGRS Domain of Rv0297 ofInternational journal of molecular sciences · 2021Article
- Enhanced catalytic activity ofHeliyon · 2020Article
- Impact of Bacterial Toxins in the Lungs.Toxins · 2020Review
- Calcium Regulation of Bacterial Virulence.Advances in experimental medicine and biology · 2020Review
- Article
- Review
- Type I Secretion Systems-One Mechanism for All?Microbiology spectrum · 2019Review
- Calcium-Dependent RTX Domains in the Development of Protein Hydrogels.Gels (Basel, Switzerland) · 2019Review
- Serralysin family metalloproteases protects Serratia marcescens from predation by the predatory bacteria Micavibrio aeruginosavorus.Scientific reports · 2018Article
- Receptor-Based Peptides for Inhibition of Leukotoxin Activity.ACS infectious diseases · 2018Article
- Review
- Type I Protein Secretion-Deceptively Simple yet with a Wide Range of Mechanistic Variability across the Family.EcoSal Plus · 2016Review
- Identification of SlpB, a Cytotoxic Protease from Serratia marcescens.Infection and immunity · 2015Article
- Interdomain Contacts and the Stability of Serralysin Protease from Serratia marcescens.PloS one · 2015Article
- Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Pseudomonas aeruginosa is an opportunistic pathogen that contributes to the mortality of immunocompromised individuals and patients with cystic fibrosis. Pseudomonas infection presents clinical challenges due to its ability to form biofilms and modulate host-pathogen interactions through the secretion of virulence factors. The calcium-regulated alkaline protease (AP), a member of the repeats in toxin (RTX) family of proteins, is implicated in multiple modes of infection. A series of full-length and truncation mutants were purified for structural and functional studies to evaluate the role of Ca(2+) in AP folding and activation. We find that Ca(2+) binding induces RTX folding, which serves to chaperone the folding of the protease domain. Subsequent association of the RTX domain with an N-terminal α-helix stabilizes AP. These results provide a basis for the Ca(2+)-mediated regulation of AP and suggest mechanisms by which Ca(2+) regulates the RTX family of virulence factors.
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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.