ArticlePloS one2012
Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Phosphorylation of Staphylococcus aureus β-lactamase, a prerequisite to its sequestration on the cytoplasmic membrane.Protein science : a publication of the Protein Society · 2025Article
- Optimization of a recombinant BlaR-CTD protein formulation using the response surface methodology.Journal of biological engineering · 2024Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Constructing and deconstructing the bacterial cell wall.Protein science : a publication of the Protein Society · 2020Review
- Development of a novel heterologous β-lactam-specific whole-cell biosensor inJournal of biological engineering · 2020Article
- An experiment-informed signal transduction model for the role of the Staphylococcus aureus MecR1 protein in β-lactam resistance.Scientific reports · 2019Article
- Article
- A novel family of soluble minimal scaffolds provides structural insight into the catalytic domains of integral membrane metallopeptidases.The Journal of biological chemistry · 2013Article
- Structure-function studies of the staphylococcal methicillin resistance antirepressor MecR2.The Journal of biological chemistry · 2013Article
- Bacterial cell-wall recycling.Annals of the New York Academy of Sciences · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Bacillus licheniformis 749/I, BlaP β-lactamase is induced by the presence of a β-lactam antibiotic outside the cell. The first step in the induction mechanism is the detection of the antibiotic by the membrane-bound penicillin receptor BlaR1 that is composed of two functional domains: a carboxy-terminal domain exposed outside the cell, which acts as a penicillin sensor, and an amino-terminal domain anchored to the cytoplasmic membrane, which works as a transducer-transmitter. The acylation of BlaR1 sensor domain by the antibiotic generates an intramolecular signal that leads to the activation of the L3 cytoplasmic loop of the transmitter by a single-point cleavage. The exact mechanism of L3 activation and the nature of the secondary cytoplasmic signal launched by the activated transmitter remain unknown. However, these two events seem to be linked to the presence of a HEXXH zinc binding motif of neutral zinc metallopeptidases. By different experimental approaches, we demonstrated that the L3 loop binds zinc ion, belongs to Gluzincin metallopeptidase superfamily and is activated by self-proteolysis.
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