Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities

Weel-Sneve, Ragnhild; Kristiansen, Knut Ivan; Odsbu, Ingvild; Dalhus, Bjørn; Booth, James A.; Rognes, Torbjørn; Skarstad, Kirsten; Bjørås, Magnar

doi:10.1371/journal.pgen.1003260

Cited by 60 publications

(73 citation statements)

References 34 publications

(39 reference statements)

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“…E. coli RalA; Guo et al, 2014), those located in the membrane either induce pores into the cell membrane (e.g. E. coli Hok; reviewed by Gerdes & Wagner, 2007), affect DNA recombination (E. coli DinQ; Weel-Sneve et al, 2013) or interfere with cell envelope synthesis (E. faecalis Fst; reviewed by Weaver, 2012). In other cases, like E. coli TisB, a role in persister formation has been demonstrated (e.g.…”

Section: Discussionmentioning

confidence: 99%

Heat-shock-induced refolding entails rapid degradation of bsrG toxin mRNA by RNases Y and J1

Jahn

Brantl

2016

Microbiology

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Gene regulation accomplished by alternative folding of an mRNA is a widely used mechanism. Classical examples are the various transcriptional attenuation mechanisms that employ, for example, leader peptide translation, or binding of a modified protein, an uncharged tRNA or an antisense RNA to the 59 untranslated region of an mRNA. With the discovery of transcriptional and translational riboswitches, it became clear that small metabolites or even metal ions can also alter RNA secondary structures and, hence, gene expression. In addition, biophysical factors like temperature can affect RNA folding, as exemplified by RNA thermometers. We have investigated in detail the type I toxin-antitoxin system bsrG/SR4 from Bacillus subtilis. The antitoxin SR4 is a cis-encoded regulatory RNA that neutralizes BsrG toxin action. SR4 prevents toxin expression by promoting degradation of the toxin mRNA and inhibiting its translation. In addition, upon temperature shock the amount of toxin mRNA decreases significantly. Here, we demonstrate that heat shock induces a refolding in the central region of the toxin mRNA that makes it more accessible to degradation by RNases Y and J1. Furthermore, we show that BsrG might play a role at the onset of stationary phase, when the antitoxin SR4 can no longer prevent toxin synthesis.

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Section: Discussionmentioning

confidence: 99%

Heat-shock-induced refolding entails rapid degradation of bsrG toxin mRNA by RNases Y and J1

Jahn

Brantl

2016

Microbiology

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“…5,12 ), the biological function of many chromosomal TA loci is still poorly understood. E. coli symE/SymR was proposed to be involved in recycling of damaged RNA generated upon SOS stress, 12,13 dinQ/AgrB in chromosome stability 14 and ralR/RalA in resistance against cell-wall inhibiting antibiotics. 15 By contrast, for E. coli tisB/IstRI and hokB/SokB as well as Streptococcus mutans fstSm/SrSm, a role in persister formation has been demonstrated.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2016

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bsrE/SR5 is a type I TA system from prophage-like element P6 of the B. subtilis chromosome. The 256 nt bsrE RNA encodes a 30 aa toxin. The antitoxin SR5 is a 163 nt antisense RNA. Both genes overlap at their 3 0 ends. Overexpression of bsrE causes cell lysis on agar plates, which can be neutralized by sr5 overexpression, whereas deletion of the chromosomal sr5 copy has no effect. SR5 is short-lived with a halflife of 7 min, whereas bsrE RNA is stable with a half-life of >80 min. The sr5 promoter is 10-fold stronger than the bsrE promoter. SR5 interacts with the 3 0 UTR of bsrE RNA, thereby promoting its degradation by recruiting RNase III. RNase J1 is the main RNase responsible for SR5 and bsrE RNA degradation, and PnpA processes an SR5 precursor to the mature RNA. Hfq stabilizes SR5, but is not required for its inhibitory function. While bsrE RNA is affected by temperature shock and alkaline stress, the amount of SR5 is significantly influenced by various stresses, among them pH, anoxia and iron limitation. Only the latter one is dependent on sigB. Both RNAs are extremely unstable upon ethanol stress due to rapid degradation by RNase Y.

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“…Some chromosome-encoded type I TA systems are involved in persister formation (17)(18)(19)(20), whereas others are involved in recycling of damaged RNA (21), DNA recombination (22), or antibiotic resistance (23). Of 14 predicted B. subtilis type I systems, 5 are located on prophages and might be required for their maintenance or overcoming metabolic or environmental stress (24).…”

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confidence: 99%

In Vitro Characterization of the Type I Toxin-Antitoxin System bsrE/SR5 from Bacillus subtilis

Meißner¹,

Jahn

Brantl

2016

Journal of Biological Chemistry

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BsrE/SR5 is a new type I toxin/antitoxin system located on the prophage-like region P6 of the Bacillus subtilis chromosome. The bsrE gene encoding a 30-amino acid hydrophobic toxin and the antitoxin gene sr5 overlap at their 3 ends by 112 bp. Overexpression of bsrE causes cell lysis on agar plates. Here, we present a detailed in vitro analysis of bsrE/SR5. The secondary structures of SR5, bsrE mRNA, and the SR5/bsrE RNA complex were determined. Apparent binding rate constants (k app ) of wild-type and mutated SR5 species with wild-type bsrE mRNA were calculated, and SR5 regions required for efficient inhibition of bsrE mRNA narrowed down. In vivo studies confirmed the in vitro data but indicated that a so far unknown RNA binding protein might exist in B. subtilis that can promote antitoxin/toxin RNA interaction. Using time course experiments, the binding pathway of SR5 and bsrE RNA was elucidated. A comparison with the previously well characterized type I TA system from the B. subtilis chromosome, bsrG/SR4, reveals similarities but also significant differences.Small regulatory RNAs (sRNAs) 3 are key players in bacterial post-transcriptional gene regulation and have been discovered in a plethora of species (reviewed in Refs. 1-3). They employ either RNA/RNA base pairing or protein binding to inhibit or activate target gene expression. A special case of base pairing sRNAs is type I antitoxins that interact with complementary mRNAs encoding small toxic peptides (reviewed in Refs. 4 and 5).Originally, type I toxin-antitoxin (TA) systems were discovered on plasmids (e.g. hok/Sok on Escherichia coli plasmid R1 (6, 7) or fst/RNAII on Enterococcus faecalis plasmid pAD1 (reviewed in Refs. 8 and 9)), in which they act as postsegregational killing systems. Subsequently, many chromosome-encoded type I TA systems were found and investigated, e. (14). They are arranged as overlapping, convergently transcribed gene pairs or as divergently transcribed gene pairs located apart. The interaction between RNA antitoxin and toxin mRNA either inhibits translation or facilitates degradation of the toxin mRNA (5). One exception is bsrG/SR4, whose antitoxin SR4 is bifunctional: it promotes degradation of the toxin mRNA and inhibits toxin translation by inducing a structural alteration around the bsrG ribosome binding site (RBS) (15). Another exception is fst/RNAII from E. faecalis, in which antitoxin binding yields a complex that stabilizes both RNAs but prevents toxin translation (16).Some chromosome-encoded type I TA systems are involved in persister formation (17-20), whereas others are involved in recycling of damaged RNA (21), DNA recombination (22), or antibiotic resistance (23). Of 14 predicted B. subtilis type I systems, 5 are located on prophages and might be required for their maintenance or overcoming metabolic or environmental stress (24). Recently, we published the first temperature-dependent type I TA system bsrG/SR4 and investigated it both in vivo and in vitro (14, 15). The 38-amino acid hydrophobic toxin BsrG causes mem...

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Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities

Cited by 60 publications

References 34 publications

Heat-shock-induced refolding entails rapid degradation of bsrG toxin mRNA by RNases Y and J1

Heat-shock-induced refolding entails rapid degradation of bsrG toxin mRNA by RNases Y and J1

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

In Vitro Characterization of the Type I Toxin-Antitoxin System bsrE/SR5 from Bacillus subtilis

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