Identification of Bacillus subtilis					σW‐dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli

Butcher, Bronwyn G.; Helmann, John D.

doi:10.1111/j.1365-2958.2006.05131.x

Cited by 177 publications

(196 citation statements)

References 44 publications

(52 reference statements)

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“…For B. subtilis, three proteins similar to SppA have been described (TepA, SppA and YqeZ; Bolhuis et al, 1999;Helmann, 2002). Both, SppA and YqeZ are s W -controlled (Huang et al, 1999;Wiegert et al, 2001), and for YqeZ a function for immunity against sublancin rather than degradation of signal peptides has been shown (Butcher & Helmann, 2006). For SppA (YteI) and TepA (YmfB), a function in degradation of proteins or (signal) peptides that are inhibitory to protein translocation has been proposed (Bolhuis et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…Genes of Bacillus subtilis controlled by the alternative extracytoplasmic function (ECF) sigma factor s W constitute an antibiosis regulon (Helmann, 2002(Helmann, , 2006 that responds to a variety of envelope stresses such as certain antibiotics (Cao et al, 2002) and antimicrobial peptides (Pietiäinen et al., 2005;Butcher & Helmann, 2006), and also alkaline shock and phage infection . Its activity is modulated by RsiW, a transmembrane anti-sigma factor that sequesters and inactivates s W .…”

Section: Introductionmentioning

confidence: 99%

“…First, B. subtilis clones suppressing the toxic effect of SdpC, a protein which is involved in a cannibalism process of killing sibling cells upon entry into the sporulation programme, were mapped to a gene now renamed as prsW (protease responsible for activating s W , formerly ypdC) (Ellermeier & Losick, 2006). It has been shown that suppression is due to constitutive activation of the s W regulon, which is known to confer resistance to the SdpC toxin in cells lacking the SdpI immunity protein (Butcher & Helmann, 2006). Second, a transposon screen with a reporter consisting of GFP fused to the amino terminus of RsiW was performed, and several transposon insertions in the prsW gene were identified that stabilize GFP-RsiW and prevent site-1 cleavage of the antisigma factor (Heinrich & Wiegert, 2006).…”

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confidence: 99%

“…2a, lanes 5-8). Spot-on-lawn assays according to a published procedure (Butcher & Helmann, 2006) showed that a sublancinproducing strain spotted onto a lawn of a sublancinnegative ecsA : : spec strain generates a larger halo than on a lawn of the corresponding ecsA wild-type strain, indicating that s W -mediated sublancin immunity is absent in the ecsA-negative strain. Similarly, treatment with vancomycin, an antibiotic that targets cell wall biosynthesis and induces the B. subtilis s W regulon (Cao et al, 2002), did not induce the s W -controlled pbpE and yuaG genes in an ecsA-negative strain, in contrast to the ecsA wild-type (data not shown).…”

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The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

et al. 2008

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The Bacillus subtilis s W regulon is induced by different stresses that most probably affect integrity of the cell envelope. The activity of the extracytoplasmic function (ECF) sigma factor s W is modulated by the transmembrane anti-sigma factor RsiW, which undergoes stress-induced degradation in a process known as regulated intramembrane proteolysis, finally resulting in the release of s W and the transcription of s W -controlled genes. Mutations in the ecsA gene, which encodes an ATP binding cassette (ABC) of an ABC transporter of unknown function, block site-2 proteolysis of RsiW by the intramembrane cleaving protease RasP (YluC). In addition, degradation of the cell division protein FtsL, which represents a second RasP substrate, is blocked in an ecsA-negative strain. The defect in s W induction of an ecsA-knockout strain could be partly suppressed by overproducing RasP. A B. subtilis rasP-knockout strain displayed the same pleiotropic phenotype as an ecsA knockout, namely defects in processing a-amylase, in competence development, and in formation of multicellular structures known as biofilms. INTRODUCTIONGenes of Bacillus subtilis controlled by the alternative extracytoplasmic function (ECF) sigma factor s W constitute an antibiosis regulon (Helmann, 2002(Helmann, , 2006 that responds to a variety of envelope stresses such as certain antibiotics (Cao et al., 2002) and antimicrobial peptides (Pietiäinen et al., 2005;Butcher & Helmann, 2006), and also alkaline shock and phage infection . Its activity is modulated by RsiW, a transmembrane anti-sigma factor that sequesters and inactivates s W . Upon a stress signal, RsiW is degraded by the mechanism of regulated intramembrane proteolysis (RIP). In a concerted action, at least three proteases in three different compartments of the cell degrade the RsiW anti-sigma factor in a sequential manner, finally resulting in the release of s W and the transcription of s Wcontrolled genes. The first protease that has been identified to be involved in that process is RasP (regulating anti-sigma factor protease; formerly YluC). RasP belongs to the group of zinc-dependent intramembrane cleaving proteases (iClips) and cleaves RsiW in its transmembrane domain after the extracytoplasmic part of the anti-sigma factor has been removed by a site-1 protease (Schöbel et al., 2004). The site-2 degradation step catalysed by RasP uncovers a cryptic proteolytic tag that ensures further degradation of the RsiW remnant by cytoplasmic proteases, mainly ClpXP (Zellmeier et al., 2006). These two steps are related to RIP of the s E anti-sigma factor RseA of Escherichia coli (Ades, 2004;Alba & Gross, 2004). RasP is an orthologue of E. coli RseP, and the concept of a cryptic proteolytic tag recognized by ClpXP was first described for that system (Akiyama et al., 2004;Flynn et al., 2004). However, there is a marked difference in the site-1 proteolytic step, because no dependency on B. subtilis Deg (Htr) proteases was found and the inducing stress is apparently different. The probable site-1 prot...

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

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“…The regulation of B. subtilis ECF s factor SigW (s W ) by its cognate anti-s factor has been investigated in detail. The s W stress response confers resistance to cell envelope perturbing agents including antibiotics and detergents (Butcher & Helmann, 2006;Ellermeier & Losick, 2006;Mascher et al, 2007), and is also activated after overproduction of membrane proteins (Zweers et al, 2009). s W is released into the cytoplasm when its anti-s factor RsiW undergoes RIP through a cascade of proteolytic events catalysed by PrsW, TSP, RasP and ClpXP or ClpEP (Heinrich et al, 2009;Ho & Ellermeier, 2012;Schöbel et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

The atypical two-subunit σ factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress

2016

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The atypical two-subunit s factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress Extracytoplasmic function (ECF) s factors constitute a major component of the physicochemical sensory apparatus in bacteria. Most ECF s factors are co-expressed with a negative regulator called an anti-s factor that binds to its cognate s factor and sequesters it from productive association with core RNA polymerase (RNAP). Anti-s factors constitute an important element of signal transduction pathways that mediate an appropriate transcriptional response to changing environmental conditions. The Bacillus subtilis genome encodes seven canonical ECF s factors and six of these are co-expressed with experimentally verified anti-s factors. B. subtilis also expresses an ECF-like atypical two-subunit s factor composed of subunits SigO and RsoA that becomes active after exposure to certain cell-wall-acting antibiotics and to growth under acidic conditions. This work describes the identification and preliminary characterization of a protein (RsiO, formerly YvrL) that constitutes the anti-s factor cognate to SigO-RsoA. Synthesis of RsiO represses SigO-RsoA-dependent transcription initiation by binding the N-terminus of SigO under neutral (pH 7) conditions. Reconstitution of the SigO-RsoA-RsiO regulatory system into a heterologous host reveals that the imposition of acid stress (pH 5.4) abolishes the ability of RsiO to repress SigO-RsoA-dependent transcription and this correlates with loss of RsiO binding affinity for SigO. A current model for RsiO function indicates that RsiO responds, either directly or indirectly, to increased extracytoplasmic hydrogen ion concentration and becomes inactivated. This results in the release of SigO into the cytoplasm, where it productively associates with RsoA and core RNAP to initiate transcription from target promoters in the cell.

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Proteolytic Activation of Extra Cytoplasmic Function (ECF) σ Factors

Hastie

Ellermeier

2016

Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria

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Identification of Bacillus subtilis σ^W‐dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli

Cited by 177 publications

References 44 publications

The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

The atypical two-subunit σ factor from Bacillus subtilis is regulated by an integral membrane protein and acid stress

Proteolytic Activation of Extra Cytoplasmic Function (ECF) σ Factors

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