ArticleMolecular microbiology2017
Structural modeling and functional analysis of the essential ribosomal processing protease Prp from Staphylococcus aureus.
Article in Molecular microbiology, 2017. 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, 12 citations in OpenAlex.
- Cleavage ofbioRxiv : the preprint server for biology · 2025Article
- Ribosomal-processing cysteine protease homolog modulatesJournal of bacteriology · 2024Article
- Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation.Journal of molecular biology · 2024Article
- Functional annotation of uncharacterized proteins from Fusobacterium nucleatum: identification of virulence factors.Genomics & informatics · 2023Article
- Phage-Related Ribosomal Proteases (Prps): Discovery, Bioinformatics, and Structural Analysis.Antibiotics (Basel, Switzerland) · 2022Article
- Phage-Related Ribosomal Protease (Prp) ofBiochemistry · 2022Article
- The ins and outs of Bacillus proteases: activities, functions and commercial significance.FEMS microbiology reviews · 2022Review
- Three overlooked key functional classes for building up minimal synthetic cells.Synthetic biology (Oxford, England) · 2021Article
- Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement.Microbial biotechnology · 2018Article
- Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80α and SaPI1 Capsids.Viruses · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In Firmicutes and related bacteria, ribosomal large subunit protein L27 is encoded with a conserved N-terminal extension that is removed to expose residues critical for ribosome function. Bacteria encoding L27 with this N-terminal extension also encode a sequence-specific cysteine protease, Prp, which carries out this cleavage. In this work, we demonstrate that L27 variants with an un-cleavable N-terminal extension, or lacking the extension (pre-cleaved), are unable to complement an L27 deletion in Staphylococcus aureus. This indicates that N-terminal processing of L27 is not only essential but possibly has a regulatory role. Prp represents a new clade of previously uncharacterized cysteine proteases, and the dependence of S. aureus on L27 cleavage by Prp validates the enzyme as a target for potential antibiotic development. To better understand the mechanism of Prp activity, we analyzed Prp enzyme kinetics and substrate preference using a fluorogenic peptide cleavage assay. Molecular modeling and site-directed mutagenesis implicate several residues around the active site in catalysis and substrate binding, and support a structural model in which rearrangement of a flexible loop upon binding of the correct peptide substrate is required for the active site to assume the proper conformation. These findings lay the foundation for the development of antimicrobials that target this novel, essential pathway.
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