ArticleProceedings of the National Academy of Sciences of the United States of America2011
Essential PcsB putative peptidoglycan hydrolase interacts with the essential FtsXSpn cell division protein in Streptococcus pneumoniae D39.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
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Who cites it
120 citing papers in PubMed, 160 citations in OpenAlex.
- Article
- Pangenome-GuidedPharmaceuticals (Basel, Switzerland) · 2026Article
- RelA-mediated (p)ppGpp accumulation links glucose starvation to peptidoglycan synthesis arrest and spherical morphogenesis via PBP2x and FtsX inJournal of bacteriology · 2026Article
- Article
- Human Milk Oligosaccharides Inhibit Group B Streptococcal Growth by Binding PcsB, an Essential Cell Wall Separation Protein.JACS Au · 2026Article
- Article
- Characterization of the cell division-associated peptidoglycan amidase AmiA ofJournal of bacteriology · 2026Article
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- Article
- Cell splitting in Staphylococcus aureus is controlled by an adaptor protein facilitating degradation of a peptidoglycan hydrolase.PLoS genetics · 2025Article
- Alleviating penicillin-resistant Streptococcus pneumoniae‑induced lung epithelial cell injury: mechanistic insights into effects of the optimized combination of main components from Yinhuapinggan granules.BMC infectious diseases · 2025Article
- Characterization of VldE (Spr1875), a Pneumococcal Two-State l,d-Endopeptidase with a Four-Zinc Cluster in the Active Site.ACS catalysis · 2024Article
- Modulation of the lytic apparatus by the FtsEX complex within the bacterial division machinery.FEBS letters · 2024Review
- Outer membrane barrier impairment byMicrobiology (Reading, England) · 2024Article
- In Situ Biofilm Affinity-Based Protein Profiling Identifies the Streptococcal Hydrolase GbpB as the Target of a Carolacton-Inspired Chemical Probe.Journal of the American Chemical Society · 2024Article
- Elongasome core proteins and class A PBP1a display zonal, processive movement at the midcell ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Structure and activity of the septal peptidoglycan hydrolysis machinery crucial for bacterial cell division.PLoS biology · 2024Article
- Secreted antigen A peptidoglycan hydrolase is essential forbioRxiv : the preprint server for biology · 2024Article
- Mycobacterial FtsEX-RipC interaction is required for normal growth and cell morphology in rifampicin and low ionic strength conditions.Microbiology spectrum · 2024Article
60 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The connection between peptidoglycan remodeling and cell division is poorly understood in ellipsoid-shaped ovococcus bacteria, such as the human respiratory pathogen Streptococcus pneumoniae. In S. pneumoniae, peptidoglycan homeostasis and stress are regulated by the WalRK (VicRK) two-component regulatory system, which positively regulates expression of the essential PcsB cysteine- and histidine-dependent aminohydrolases/peptidases (CHAP)-domain protein. CHAP-domain proteins usually act as peptidoglycan hydrolases, but purified PcsB lacks detectable enzymatic activity. To explore the functions of PcsB, its subcellular localization was determined. Fractionation experiments showed that cell-bound PcsB was located through hydrophobic interactions on the external membrane surface of pneumococcal cells. Immunofluorescent microscopy localized PcsB mainly to the septa and equators of dividing cells. Chemical cross-linking combined with immunoprecipitation showed that PcsB interacts with the cell division complex formed by membrane-bound FtsX(Spn) and cytoplasmic FtsE(Spn) ATPase, which structurally resemble an ABC transporter. Far Western blotting showed that this interaction was likely through the large extracellular loop of FtsX(Spn) and the amino terminal coiled-coil domain of PcsB. Unlike in Bacillus subtilis and Escherichia coli, we show that FtsX(Spn) and FtsE(Spn) are essential in S. pneumoniae. Consistent with an interaction between PcsB and FtsX(Spn), cells depleted of PcsB or FtsX(Spn) had strikingly similar defects in cell division, and depletion of FtsX(Spn) caused mislocalization of PcsB but not the FtsZ(Spn) early-division protein. A model is presented in which the interaction of the FtsEX(Spn) complex with PcsB activates its peptidoglycan hydrolysis activity and couples peptidoglycan remodeling to pneumococcal cell division.
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