ArticleJournal of molecular biology2022
Identification of Functional Spo0A Residues Critical for Sporulation in Clostridioides difficile.
Article in Journal of molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Clostridioides difficile pathogenesis and control.Nature reviews. Microbiology · 2026Review
- Deciphering strain differences in codY regulation ofMicrobiology spectrum · 2026Article
- Nanoluciferase-Based Reporters for Clostridioides difficile.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Pxp Complex Detoxifies 5-Oxoproline and Promotes the Growth of Clostridioides difficile.Molecular microbiology · 2025Article
- A metabolite dehydrogenase pathway represses sporulation of Clostridioides difficile.Anaerobe · 2025Article
- Uncovering newMicrobiology spectrum · 2024Article
- The small acid-soluble proteins of Clostridioides difficile regulate sporulation in a SpoIVB2-dependent manner.PLoS pathogens · 2024Article
- The small acid-soluble proteins ofbioRxiv : the preprint server for biology · 2024Article
- A conserved switch controls virulence, sporulation, and motility in C. difficile.PLoS pathogens · 2024Article
- Review
- The pH-responsive SmrR-SmrT system modulatesInfection and immunity · 2024Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- Whole genome sequencing provides evidence for Bacillus velezensis SH-1471 as a beneficial rhizosphere bacterium in plants.Scientific reports · 2023Article
- The RgaS-RgaR two-component system promotes Clostridioides difficile sporulation through a small RNA and the Agr1 system.PLoS genetics · 2023Article
- The RgaS-RgaR two-component system promotesbioRxiv : the preprint server for biology · 2023Article
- Non-Toxin-BasedPathogens (Basel, Switzerland) · 2023Article
- Review
- Comparative biofilm-forming ability betweenFrontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Clostridioides difficile is an anaerobic, Gram-positive pathogen that is responsible for C. difficile infection (CDI). To survive in the environment and spread to new hosts, C. difficile must form metabolically dormant spores. The formation of spores requires activation of the transcription factor Spo0A, which is the master regulator of sporulation in all endospore-forming bacteria. Though the sporulation initiation pathway has been delineated in the Bacilli, including the model spore-former Bacillus subtilis, the direct regulators of Spo0A in C. difficile remain undefined. C. difficile Spo0A shares highly conserved protein interaction regions with the B. subtilis sporulation proteins Spo0F and Spo0A, although many of the interacting factors present in B. subtilis are not encoded in C. difficile. To determine if comparable Spo0A residues are important for C. difficile sporulation initiation, site-directed mutagenesis was performed at conserved receiver domain residues and the effects on sporulation were examined. Mutation of residues important for homodimerization and interaction with positive and negative regulators of B. subtilis Spo0A and Spo0F impacted C. difficile Spo0A function. The data also demonstrated that mutation of many additional conserved residues altered C. difficile Spo0A activity, even when the corresponding Bacillus interacting proteins are not apparent in the C. difficile genome. Finally, the conserved aspartate residue at position 56 of C. difficile Spo0A was determined to be the phosphorylation site that is necessary for Spo0A activation. The finding that Spo0A interacting motifs maintain functionality suggests that C. difficile Spo0A interacts with yet unidentified proteins that regulate its activity and control spore formation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.