A multistress responsive type I toxin-antitoxin system:<i>bsrE</i>/SR5 from the<i>B. subtilis</i>chromosome

Müller, Peter; Jahn, Natalie; Ring, Christiane; Maiwald, Caroline; Neubert, Robert J.; Meißner, Christin; Brantl, Sabine

doi:10.1080/15476286.2016.1156288

Cited by 35 publications

(86 citation statements)

References 48 publications

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“…Therefore, we used to test our assumption as first substrate the small (162 nt) internally labeled sRNA SR5, the antitoxin of a type I toxin-antitoxin system investigated in our group. SR5 has a 2-fold longer half-life in a Δ rnjA strain, whereas its half-life was not affected by RNase Y 32 . In an in vitro degradation assay (Fig.…”

Section: Resultsmentioning

confidence: 96%

Dual-function sRNA encoded peptide SR1P modulates moonlighting activity of B. subtilis GapA

Gimpel

Brantl

2016

RNA Biology

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SR1 is a dual-function sRNA from B. subtilis that acts as a base-pairing regulatory RNA and as a peptide-encoding mRNA. Both functions of SR1 are highly conserved. Previously, we uncovered that the SR1 encoded peptide SR1P binds the glycolytic enzyme GapA resulting in stabilization of gapA mRNA. Here, we demonstrate that GapA interacts with RNases Y and J1, and this interaction was RNA-independent. About 1% of GapA molecules purified from B. subtilis carry RNase J1 and about 2% RNase Y. In contrast to the GapA/RNase Y interaction, the GapA/RNaseJ1 interaction was stronger in the presence of SR1P. GapA/SR1P-J1/Y displayed in vitro RNase activity on known RNase J1 substrates. Moreover, the RNase J1 substrate SR5 has altered half-lives in a ΔgapA strain and a Δsr1 strain, suggesting in vivo functions of the GapA/SR1P/J1 interaction. Our results demonstrate that the metabolic enzyme GapA moonlights in recruiting RNases while GapA bound SR1P promotes binding of RNase J1 and enhances its activity.

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Section: Resultsmentioning

confidence: 96%

Dual-function sRNA encoded peptide SR1P modulates moonlighting activity of B. subtilis GapA

Gimpel

Brantl

2016

RNA Biology

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“…For the construction of transcriptional lacZ fusions, PCR fragments were obtained on chromosomal DNA as template with primer pairs SB2744/2745 and SB2746/2747, digested with BamHI and EcoRI and inserted into pMG16 [56] cleaved with the same enzyme pair yielding pMGP21 (p rocABC ) and pMGP22 (p rocDEF ), respectively. For the construction of translational lacZ fusions, PCR fragments were generated with primer pairs SB2774/SB2775 (ccpN), SB2778/SB2779 (rocA) and SB2780/ SB2781 (rocD), cleaved with BamHI and EcoRI and inserted into the BamHI/EcoRI pGAB1 vector resulting in pGABP1-3, respectively.…”

Section: Construction Of Transcriptional and Translational Lacz Fusiomentioning

confidence: 99%

A new role for CsrA: promotion of complex formation between an sRNA and its mRNA target in Bacillus subtilis

et al. 2019

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“…Regulation of type I TA systems in response to stress has been observed in other species. For the bsrE/SR5 type I system of B. subtilis, the SR5 antitoxin is affected by pH, anoxia and iron limitation while the BsrE toxin is sensitive to temperature shock and alkaline stress (42). In S. aureus, the SprA1/SprA1AS system is induced in response to acidic or oxidative stresses (35) reports are difficult to compare since no standard procedure was used and analysis was most of the time performed after more than a week exposure to stress (17,37,44).…”

Section: Discussionmentioning

confidence: 99%

A peptide of a type I toxin-antitoxin system induces Helicobacter pylori morphological transformation from spiral-shape to coccoids

Mortaji

Tejada-Arranz

Rifflet

et al. 2019

Preprint

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25 26 suggesting coccoid viability. Using single-cell live microscopy, we observed that shape 42 conversion is associated with cell division interference. Oxidative stress represses antitoxin 43 promoter activity and enhances processing of its transcript leading to an imbalanced ratio in 44 favor of AapA1 toxin expression. 45Our data are in favor of viable coccoids with characteristics of dormant bacteria that might 46 be important in H. pylori infections refractory to treatment. 47 Significance Statement 49Helicobacter pylori, a gastric pathogen responsible for 800,000 deaths in the world every 50year, is encountered, both in vitro and in patients, as spiral-shaped bacteria and as round cells 51 named coccoids. We discovered that the toxin from a chromosomal type I toxin-antitoxin 52 system is targeting H. pylori membrane and acting as an effector of the morphological 53 conversion of H. pylori to coccoids. We showed that these round cells maintain their 54 membrane integrity and metabolism, strongly suggesting that they are viable dormant bacteria. 55Oxidative stress was identified as a signal inducing toxin expression. Our findings reveal new 56 insights into a form of dormancy of this bacterium that might be associated with H. pylori 57 infections refractory to treatment. 58 59 60 (10) and it was more generally found that decreased intracellular ATP concentration is a 79 landmark of persister formation (11). 80In the present work, we explored the role of TA systems in Helicobacter pylori, a 81 bacterium that colonizes the stomach of half of the human population worldwide and causes 82 the development of gastritis. In some cases, gastritis evolves into peptic ulcer disease or 83 gastric carcinoma that causes about 800,000 deaths in the world every year (12, 13). This 84 microaerophilic bacterium is unique in its capacity to persistently colonize the stomach 85 despite its extreme acidity and intense immune response (13). The molecular mechanisms at 86 both translation inhibition of the AapA1 active message and leading to rapid degradation of 104 the duplex by RNase III has been recently published (20). The H. pylori type I toxins are 105 typically small hydrophobic peptides of 30-40 amino acids predicted to form alpha-helices. 106No clues on the mode of action or the physiological role of these systems have been reported. 107Here we show that the AapA1 toxin induces a rapid and massive morphological 108 transformation of H. pylori from spirals to coccoids by targeting the inner membrane and 109 interfering with cell division, and that oxidative stress triggers imbalanced expression of the 110 TA components in favor of toxin production. 111 Results 112IsoA1 or pA1*. In contrast, addition of the inducer causes a rapid and immediate growth 129 arrest of H. pylori with pA1 indicating a toxic effect of AapA1 expression (Fig. 1B). The 130 growth arrest was accompanied by loss of culturability of more than 10 4 -fold 8h after 131 induction. 132In parallel to growth, we investigated the consequences of AapA1 expressio...

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A multistress responsive type I toxin-antitoxin system:bsrE/SR5 from theB. subtilischromosome

Cited by 35 publications

References 48 publications

Dual-function sRNA encoded peptide SR1P modulates moonlighting activity of B. subtilis GapA

Dual-function sRNA encoded peptide SR1P modulates moonlighting activity of B. subtilis GapA

A new role for CsrA: promotion of complex formation between an sRNA and its mRNA target in Bacillus subtilis

A peptide of a type I toxin-antitoxin system induces Helicobacter pylori morphological transformation from spiral-shape to coccoids

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