ArticleThe Journal of biological chemistry2012
The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.
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 53 papers.
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Who cites it
53 citing papers in PubMed, 90 citations in OpenAlex.
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- The serine protease HtrA regulates Group B Streptococcus virulence and affects the host response to infection.PLoS pathogens · 2025Article
- Deciphering the role of SMU.1147 in peptide-mediated signaling and competence inMicrobiology spectrum · 2025Article
- Competence Regulation inCurrent medicinal chemistry · 2025Review
- Comparative analysis of theFrontiers in microbiology · 2025Article
- Time-resolved RNA-seq analysis to unravel theMicrobiology spectrum · 2024Article
- Noncanonical Streptococcus sanguinis ComCDE circuitry integrates environmental cues in transformation outcome decision.Cell chemical biology · 2024Article
- Diverse regulatory pathways modulate bet hedging of competence induction in epigenetically-differentiated phase variants of Streptococcus pneumoniae.Nucleic acids research · 2023Article
- Fever-like temperature bursts promote competence development via an HtrA-dependent pathway in Streptococcus pneumoniae.PLoS genetics · 2023Article
- The involvement of CiaR and the CiaR-regulated serine protease HtrA in thermal adaptation ofMicrobiology (Reading, England) · 2023Article
- The Outer Surface Protease, SepM, Is Required forJournal of bacteriology · 2022Article
- Investigating theMicrobiology (Reading, England) · 2022Article
- The acquisition of clinically relevant amoxicillin resistance in Streptococcus pneumoniae requires ordered horizontal gene transfer of four loci.PLoS pathogens · 2022Article
- Competence shut-off by intracellular pheromone degradation in salivarius streptococci.PLoS genetics · 2022Article
- Pneumococcal capsule blocks protection by immunization with conserved surface proteins.NPJ vaccines · 2021Article
- Pathogenicity and virulence ofVirulence · 2021Review
- Three Distinct Proteases Are Responsible for Overall Cell Surface Proteolysis in Streptococcus thermophilus.Applied and environmental microbiology · 2021Article
- New Insights into Beta-Lactam Resistance ofMicroorganisms · 2021Article
- Article
- Pneumococcal Extracellular Serine Proteases: Molecular Analysis and Impact on Colonization and Disease.Frontiers in cellular and infection microbiology · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The HtrA protease of Streptococcus pneumoniae functions both in a general stress response role and as an error sensor that specifically represses genetic competence when the overall level of biosynthetic errors in cellular proteins is low. However, the mechanism through which HtrA inhibits development of competence has been unknown. We found that HtrA digested the pneumococcal competence-stimulating peptide (CSP) and constituted the primary extracytoplasmic CSP-degrading activity in cultures of S. pneumoniae. Mass spectrometry demonstrated that cleavage predominantly followed residue Phe-8 of the CSP-1 isoform of the peptide within its central hydrophobic patch, and in competition assays, both CSP-1 and CSP-2 interacted with HtrA with similar efficiencies. More generally, analysis of β-casein digestion and of digestion within HtrA itself revealed a preference for substrates with non-polar residues at the P1 site. Consistent with a specificity for exposed hydrophobic residues, competition from native BSA only weakly inhibited digestion of CSP, but denaturation converted BSA into a strong competitive inhibitor of such proteolysis. Together these findings support a model in which digestion of CSP by HtrA is reduced in the presence of other unfolded proteins that serve as alternative targets for degradation. Such competition may provide a mechanism by which HtrA functions in a quality control capacity to monitor the frequency of biosynthetic errors that result in protein misfolding.
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