Alkaline shock induces the <i>Bacillus subtilis</i>σ<sup>W</sup> regulon

Wiegert, Thomas; Homuth, Georg; Versteeg, Saskia; Schumann, Wolfgang

doi:10.1046/j.1365-2958.2001.02489.x

Cited by 185 publications

(226 citation statements)

References 34 publications

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“…Similar to the results obtained with lacZ reportergene expression, we found that the number of YuaG-CFP foci (in strain DB015) increased dramatically during stationary phase (Table 2). The number of YuaG foci also increased upon alkaline stress (data not shown), suggesting increased expression under these conditions, as described previously (Wiegert et al, 2001). We also analysed the expression of YuaG-CFP in a strain background lacking sigW (strain DB016) and found that YuaG-CFP foci were present in the stationary phase, comparable to wild-type cells (data not shown).…”

Section: Quantification Of Yuag Expression In Vivosupporting

confidence: 83%

“…With the pMUTIN4 integration, we had a tool in hand that allowed assaying the transcription of YuaG during growth of strain DB003. Integration of pMUTIN4 places the lacZ gene under the control of the native yuaG promoter, which is in front of yuaF (Wiegert et al, 2001). Growing cells were collected at different time points and b-galactosidase activity was measured.…”

Section: Quantification Of Yuag Expression In Vivomentioning

confidence: 99%

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Characterization and subcellular localization of a bacterial flotillin homologue

2009

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The process of endospore formation in Bacillus subtilis is complex, requiring the generation of two distinct cell types, a forespore and larger mother cell. The development of these cell types is controlled and regulated by cell type-specific gene expression, activated by a s-factor cascade. Activation of these cell type-specific sigma factors is coupled with the completion of polar septation. Here, we describe a novel protein, YuaG, a eukaryotic reggie/flotillin homologue that is involved in the early stages of sporulation of the Gram-positive model organism B. subtilis. YuaG localizes in discrete foci in the membrane and is highly dynamic. Purification of detergent-resistant membranes revealed that YuaG is associated with negatively charged phospholipids, e.g. phosphatidylglycerol (PG) or cardiolipin (CL). However, localization of YuaG is not always dependent on PG/CL in vivo. A yuaG disruption strain shows a delay in the onset of sporulation along with reduced sporulation efficiency, where the spores develop to a certain stage and then appear to be trapped at this stage. Our results indicate that YuaG is involved in the early stage of spore development, probably playing a role in the signalling cascade at the onset of sporulation.

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Section: Quantification Of Yuag Expression In Vivosupporting

confidence: 83%

Section: Quantification Of Yuag Expression In Vivomentioning

confidence: 99%

Characterization and subcellular localization of a bacterial flotillin homologue

2009

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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%

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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“…These include the heat-shock factor RpoH and stationary-phase protein RpoS of Escherichia coli (Morita et al, 1999;Weber et al, 2005), the general stress-response protein SigB of Bacillus subtilis (Peterson et al, 2001;Price et al, 2001;Price, 2002) and ECF (extracytoplasmic function) sigmas such as SigE of Streptomyces coelicolor, RpoE of E. coli and SigW of B. subtilis (Lonetto et al, 1994;Raina et al, 1995;Rouviere et al, 1995;De La Penas et al, 1997;Wiegert et al, 2001). …”

Section: Introductionmentioning

confidence: 99%

Regulatory role of RsgI in sigI expression in Bacillus subtilis

et al. 2007

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The sigma gene, sigI, of Bacillus subtilis belongs to the group IV heat-shock response genes and has many orthologues in the bacterial phylum Firmicutes. The B. subtilis sigI gene is considered to constitute an operon with rsgI (regulation of sigI, formerly ykrI). As little is known about either the structure and function of the sigI-rsgI operon or the SigI regulons, the role of RsgI in heat-inducible transcription of the sigI-rsgI operon was investigated, using Northern analysis and a heat-stable b-galactosidase reporter assay. Heat-inducible, SigI-dependent transcription of the sigI-rsgI operon was stimulated greatly by disrupting rsgI. Yeast two-hybrid analysis showed direct interaction between the N-terminal portion of the presumed RsgI protein and SigI. Without RsgI function, induction of transcription of the sigI-rsgI operon upon transient heat stress depended on dnaK activity. However, transcription of the operon was induced during growth at prolonged higher temperature even without DnaK function. Without RsgI function, sigI-rsgI operon transcription was induced after the end of growth independent of any temperature shift in a sporulation medium and toward the end of growth in a rich complex medium. Furthermore, glucose addition resulted in a strong suppression of sigI-rsgI transcription. Therefore it is hypothesized that transcription of the sigI-rsgI operon of B. subtilis is negatively regulated by the putative transmembrane protein RsgI, which moderates SigI's sensitivity to heat shock or nutritional stress.

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Alkaline shock induces the Bacillus subtilisσ^W regulon

Cited by 185 publications

References 34 publications

Characterization and subcellular localization of a bacterial flotillin homologue

Characterization and subcellular localization of a bacterial flotillin homologue

The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

Regulatory role of RsgI in sigI expression in Bacillus subtilis

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Alkaline shock induces the Bacillus subtilisσW regulon

Cited by 185 publications

References 34 publications

Characterization and subcellular localization of a bacterial flotillin homologue

Characterization and subcellular localization of a bacterial flotillin homologue

The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

Regulatory role of RsgI in sigI expression in Bacillus subtilis

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Alkaline shock induces the Bacillus subtilisσ^W regulon