ArticleJournal of bacteriology2003
Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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49 citing papers in PubMed, 109 citations in OpenAlex.
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- A fitness trade-off between growth and survival governed by Spo0A-mediated proteome allocation constraints inScience advances · 2023Article
- Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host interactions.Cell chemical biology · 2023Review
- Second-Generation Transfer Mediates Efficient Propagation of ICEJournal of bacteriology · 2022Article
- Exploring the Bile Stress Response ofMolecules (Basel, Switzerland) · 2021Article
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- Cell morphology maintenance in Bacillus subtilis through balanced peptidoglycan synthesis and hydrolysis.Scientific reports · 2020Article
- Bacterial nanotubes as a manifestation of cell death.Nature communications · 2020Article
- The role of the bacterial protease Prc in the uropathogenesis of extraintestinal pathogenic Escherichia coli.Journal of biomedical science · 2020Article
- Glucose-Mediated Protein Arginine Phosphorylation/Dephosphorylation RegulatesFrontiers in microbiology · 2020Article
- Homeostatic control of cell wall hydrolysis by the WalRK two-component signaling pathway ineLife · 2019Article
- Distinct and Specific Role of NlpC/P60 Endopeptidases LytA and LytB in Cell Elongation and Division ofFrontiers in microbiology · 2019Article
- In silico characterization of the global Geobacillus and Parageobacillus secretome.Microbial cell factories · 2018Article
- Solution scattering study of the Bacillus subtilis PgdS enzyme involved in poly-γ-glutamic acids degradation.PloS one · 2018Article
- Metabolism Shapes the Cell.Journal of bacteriology · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LytF, LytE, and LytC are vegetative cell wall hydrolases in Bacillus subtilis. Immunofluorescence microscopy showed that an epitope-tagged LytF fusion protein (LytF-3xFLAG) in the wild-type background strain was localized at cell separation sites and one of the cell poles of rod-shaped cells during vegetative growth. However, in a mutant lacking both the cell surface protease WprA and the extracellular protease Epr, the fusion protein was observed at both cell poles in addition to cell separation sites. This suggests that LytF is potentially localized at cell separation sites and both cell poles during vegetative growth and that WprA and Epr are involved in LytF degradation. The localization pattern of LytE-3xFLAG was very similar to that of LytF-3xFLAG during vegetative growth. However, especially in the early vegetative growth phase, there was a remarkable difference between the shape of cells expressing LytE-3xFLAG and the shape of cells expressing LytF-3xFLAG. In the case of LytF-3xFLAG, it seemed that the signals in normal rod-shaped cells were stronger than those in long-chain cells. In contrast, the reverse was found in the case of LytE-3xFLAG. This difference may reflect the dependence on different sigma factors for gene expression. The results support and extend the previous finding that LytF and LytE are cell-separating enzymes. On the other hand, we observed that cells producing LytC-3xFLAG are uniformly coated with the fusion protein after the middle of the exponential growth phase, which supports the suggestion that LytC is a major autolysin that is not associated with cell separation.
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