Nutritional Factors Influencing the Development of Competence in the
            <i>Bacillus subtilis</i>
            Transformation System

Summary Toxin‐antitoxin modules are gene pairs encoding a toxin and its antitoxin, and are found on the chromosomes of many bacteria, including pathogens. Here, we characterize the specific contribution of the TxpA and YqcG toxins in elimination of defective cells from developing Bacillus subtilis biofilms. On nutrient limitation, defective cells accumulated in the biofilm breaking its symmetry. Deletion of the toxins resulted in accumulation of morphologically abnormal cells, and interfered with the proper development of the multicellular community. Dual physiological responses are of significance for TxpA and YqcG activation: nitrogen deprivation enhances the transcription of both TxpA and YqcG toxins, and simultaneously sensitizes the biofilm cells to their activity. Furthermore, we demonstrate that while both toxins when overexpressed affect the morphology of the developing biofilm, the toxin TxpA can act to lyse and dissolve pre‐established B. subtilis biofilms.

show abstract

“…Transformation of B. subtilis PY79 with linearized plasmid or PCR products, was performed as previously described (Wilson and Bott, 1968).…”

Section: Construction Of Strainsmentioning

confidence: 99%

Toxin‐Antitoxin systems eliminate defective cells and preserve symmetry in Bacillus subtilis biofilms

Bloom-Ackermann

Steinberg

Rosenberg

et al. 2016

Environmental Microbiology

View full text Add to dashboard Cite

show abstract

“…All experiments were performed with strains derived by transformation of the prototrophic laboratory strain PY79 (Youngman et al, 1984). Competent B. subtilis cells were prepared as previously described (Wilson and Bott, 1968). Details regarding strain and plasmid sources and construction are provided in supplemental materials.…”

Section: Strain and Plasmid Constructionmentioning

confidence: 99%

A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels

Camp¹,

Losick²

2008

Molecular Microbiology

151

View full text Add to dashboard Cite

SummaryDuring spore formation in Bacillus subtilis, s E -directed gene expression in the mother-cell compartment of the sporangium triggers the activation of s G in the forespore by a pathway of intercellular signalling that is composed of multiple proteins of unknown function. Here, we confirm that the vegetative protein SpoIIIJ, the forespore protein SpoIIQ and eight membrane proteins (SpoIIIAA through SpoIIIAH) produced in the mother cell under the control of s E are ordinarily required for intercellular signalling. In contrast, an anti-s G factor previously implicated in the pathway is shown to be dispensable. We also present evidence suggesting that SpoIIIJ is a membrane protein translocase that facilitates the insertion of SpoIIIAE into the membrane. In addition, we report the isolation of a mutation that partially bypasses the requirement for SpoIIIJ and for SpoIIIAA through SpoIIIAG, but not for SpoIIIAH or SpoIIQ, in the activation of s G . We therefore propose that under certain genetic conditions, SpoIIIAH and SpoIIQ can constitute a minimal pathway for the activation of s G . Finally, based on the similarity of SpoIIIAH to a component of type III secretion systems, we speculate that signalling is mediated by a channel that links the mother cell to the forespore.

show abstract

“…Strains are otherwise isogenic derivatives of B. subtilis PY79 (Youngman et al, 1984). B. subtilis competent cells were prepared as described previously (Wilson and Bott, 1968). The spoVM-gfp fusion at amyE was created by cloning spoVM open reading frame and 400 bases of upstream sequence into pKL147 as described previously (van Ooij and Losick, 2003) to create pKC1.…”

Section: Strain Constructionmentioning

confidence: 99%

Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis

Ramamurthi

Clapham

Losick³

2006

Molecular Microbiology

118

View full text Add to dashboard Cite

SummarySpore formation in Bacillus subtilis involves the formation of a thick, proteinaceous shell or coat that is assembled around a specialized membrane known as the outer forespore membrane. Here we present evidence that the assembling coat is tethered to the outer forespore membrane by a 26-amino-acid peptide called SpoVM, which is believed to form an amphipathic helix. We show that proper localization of SpoVM is dependent on SpoIVA, a morphogenetic protein that forms the basement layer of the spore coat, and conversely, that proper localization of SpoIVA is dependent on SpoVM. Genetic, biochemical and cytological evidence indicates that this mutual dependence is mediated in part by contact between an amino acid side-chain located near the extreme C-terminus of SpoIVA and an amino acid side-chain on the hydrophilic face of the SpoVM helix. Evidence is also presented that SpoVM adheres to the outer forespore membrane via hydrophobic, amino acid side-chains on the hydrophobic face of the helix. The results suggest that the SpoVM helix is oriented parallel to the membrane with the hydrophobic face buried in the lipid bilayer.

show abstract

Nutritional Factors Influencing the Development of Competence in the Bacillus subtilis Transformation System

Cited by 188 publications

References 12 publications

Toxin‐Antitoxin systems eliminate defective cells and preserve symmetry in Bacillus subtilis biofilms

Toxin‐Antitoxin systems eliminate defective cells and preserve symmetry in Bacillus subtilis biofilms

A novel pathway of intercellular signalling in Bacillus subtilis involves a protein with similarity to a component of type III secretion channels

Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis

Contact Info

Product

Resources

About