Small Untranslated RNA Antitoxin in<i>Bacillus subtilis</i>

Silvaggi, Jessica M.; Perkins, John B.; Losick, Richard

doi:10.1128/jb.187.19.6641-6650.2005

Cited by 147 publications

(207 citation statements)

References 32 publications

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“…The corresponding ORFs were expressed in E. coli under control of the inducible promoter P Bad . In contrast to TxpA from Bacillus subtilis which is not toxic in E. coli and does not induce lysis, 27 the expression of TxpA from E. faecalis V583 provoked cell death without lysis ( Fig. S2 and data not shown), showing the toxic effect of the protein.…”

Section: Resultsmentioning

confidence: 95%

“…5,[20][21][22][23] TA-I toxins, such as TxpA, are generally small hydrophobic proteins forming pores in membranes. 5,[24][25][26][27] Type II TA systems (TA-II) are usually made up by a bicistronic operon encoding the antitoxin protein that interacts with the toxin and inactivates its deleterious effects. Generally, TA-II toxin and antitoxin repress their own transcription via 'conditional cooperativity', a process relying on the DNA-binding properties of the antitoxin, the affinity between the toxin and the antitoxin, and their limited abundance.…”

Section: Introductionmentioning

confidence: 99%

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Regulatory crosstalk between type I and type II toxin-antitoxin systems in the human pathogen Enterococcus faecalis

et al. 2015

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We discovered a chromosomal locus containing 2 toxin-antitoxin modules (TAs) with an antisense transcriptional organization in the E. faecalis clinical isolate V583. These TAs are homologous to the type I txpA-ratA system and the type II mazEF, respectively. We have shown that the putative MazF is toxic for E. coli and triggers RNA degradation, and its cognate antitoxin MazE counteracts toxicity. The second module, adjacent to mazEF, expresses a toxin predicted to belong to the TxpA type I family found in Firmicutes, and the antisense RNA antidote, RatA. Genomic analysis indicates that the cis-association of mazEF and txpA-ratA modules has been favored during evolution, suggesting a selective advantage for this TA organization in the E. faecalis species. We showed regulatory interplays between the 2 modules, involving transcription control and RNA stability. Remarkably, our data reveal that MazE and MazEF have a dual transcriptional activity: they act as autorepressors and activate ratA transcription, most likely in a direct manner. RatA controls txpA RNA levels through stability. Our data suggest a pivotal role of MazEF in the coordinated expression of mazEF and txpA-ratA modules in V583. To our knowledge, this is the first report describing a crosstalk between type I and II TAs.

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Section: Resultsmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Regulatory crosstalk between type I and type II toxin-antitoxin systems in the human pathogen Enterococcus faecalis

et al. 2015

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“…The two respective RNA species overlap by 120 nucleotides and interact via a so-called kissing loop interaction. This interaction between txpA mRNA and the ratA RNA promotes degradation of the duplex in an RNase III-dependent manner (53,110,111). In the absence of ratA, the toxic TxpA peptide can be translated, which causes cell lysis.…”

Section: Independently Expressed Small Rnas and Rna Antitoxinsmentioning

confidence: 99%

Regulatory RNAs in Bacillus subtilis: a Gram-Positive Perspective on Bacterial RNA-Mediated Regulation of Gene Expression

Mars

Nicolas

Denham

et al. 2016

Microbiol Mol Biol Rev

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SUMMARY Bacteria can employ widely diverse RNA molecules to regulate their gene expression. Such molecules include trans -acting small regulatory RNAs, antisense RNAs, and a variety of transcriptional attenuation mechanisms in the 5′ untranslated region. Thus far, most regulatory RNA research has focused on Gram-negative bacteria, such as Escherichia coli and Salmonella . Hence, there is uncertainty about whether the resulting insights can be extrapolated directly to other bacteria, such as the Gram-positive soil bacterium Bacillus subtilis . A recent study identified 1,583 putative regulatory RNAs in B. subtilis , whose expression was assessed across 104 conditions. Here, we review the current understanding of RNA-based regulation in B. subtilis , and we categorize the newly identified putative regulatory RNAs on the basis of their conservation in other bacilli and the stability of their predicted secondary structures. Our present evaluation of the publicly available data indicates that RNA-mediated gene regulation in B. subtilis mostly involves elements at the 5′ ends of mRNA molecules. These can include 5′ secondary structure elements and metabolite-, tRNA-, or protein-binding sites. Importantly, sense-independent segments are identified as the most conserved and structured potential regulatory RNAs in B. subtilis . Altogether, the present survey provides many leads for the identification of new regulatory RNA functions in B. subtilis .

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“…Although the B. subtilis ymaH gene encodes a protein homologous to Hfq, this protein is not required for FsrAmediated inhibition of Sdh expression because a fur ymaH double mutant does not regain the ability to grow on succinate. To date, the function of Hfq remains unclear in B. subtilis and it is apparently not needed for the function of other known sRNAs (37,38). Perhaps because of the extensive sequence complementarity between FsrA and the sdhC mRNA (Fig.…”

Section: Iron-sparing Response Reduces Cellular Iron Demand and Is Admentioning

confidence: 99%

The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins

Gaballa

Antelmann

Aguilar

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

203

240

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Regulation of bacterial iron homeostasis is often controlled by the iron-sensing ferric uptake repressor (Fur). The Bacillus subtilis Fur protein acts as an iron-dependent repressor for siderophore biosynthesis and iron transport proteins. Here, we demonstrate that Fur also coordinates an iron-sparing response that acts to repress the expression of iron-rich proteins when iron is limiting. When Fur is inactive, numerous iron-containing proteins are downregulated, including succinate dehydrogenase, aconitase, cytochromes, and biosynthetic enzymes for heme, cysteine, and branched chain amino acids. As a result, a fur mutant grows slowly in a variety of nutrient conditions. Depending on the growth medium, rapid growth can be restored by mutations in one or more of the molecular effectors of the iron-sparing response. These effectors include the products of three Fur-regulated operons that encode a small RNA (FsrA) and three small, basic proteins (FbpA, FbpB, and FbpC). Extensive complementarity between FsrA and the leader region of the succinate dehydrogenase operon is consistent with an RNA-mediated translational repression mechanism for this target. Thus, iron deprivation in B. subtilis activates pathways to remodel the proteome to preserve iron for the most critical cellular functions.

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Small Untranslated RNA Antitoxin inBacillus subtilis

Cited by 147 publications

References 32 publications

Regulatory crosstalk between type I and type II toxin-antitoxin systems in the human pathogen Enterococcus faecalis

Regulatory crosstalk between type I and type II toxin-antitoxin systems in the human pathogen Enterococcus faecalis

Regulatory RNAs in Bacillus subtilis: a Gram-Positive Perspective on Bacterial RNA-Mediated Regulation of Gene Expression

The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins

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