Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis

Elsholz, Alexander K. W.; Birk, Marlène S; Charpentier, Emmanuelle; Turgay, Kürşad

doi:10.3389/fmolb.2017.00044

Cited by 43 publications

(40 citation statements)

References 172 publications

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“…). However, since a Δ clpX deletion strain displays a considerable growth defect and a pleiotropic phenotype with both Spx dependent and independent regulated traits (Elsholz et al , ), we aimed to confirm the Spx‐dependent regulation of selected genes in independent experiments by RT‐qPCR (Fig. B–D).…”

Section: Resultsmentioning

confidence: 99%

“…The heat shock response of the Gram‐positive model organism Bacillus subtilis is controlled by multiple regulators (Hecker et al , ; Elsholz et al , ). Two heat‐sensitive transcriptional repressors, HrcA and CtsR, control the expression of chaperone systems of the Hsp60 (GroESL) and Hsp40/70 (DnaKJ/GrpE) families, or the Hsp100/Clp unfoldase/protease systems ClpCP, ClpXP and ClpEP respectively (Mogk et al , ; Krüger and Hecker, ; Wiegert and Schumann, ; Elsholz et al , ).…”

Section: Introductionmentioning

confidence: 99%

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Spx, the central regulator of the heat and oxidative stress response in B. subtilis, can repress transcription of translation‐related genes

Schäfer

Heinz

Sudzinová

et al. 2018

Molecular Microbiology

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Spx is a Bacillus subtilis transcription factor that interacts with the alpha subunits of RNA polymerase. It can activate the thiol stress response regulon and interfere with the activation of many developmental processes. Here, we show that Spx is a central player orchestrating the heat shock response by up-regulating relevant stress response genes as revealed by comparative transcriptomic experiments. Moreover, these experiments revealed the potential of Spx to inhibit transcription of translation-related genes. By in vivo and in vitro experiments, we confirmed that Spx can inhibit transcription from rRNA. This inhibition depended mostly on UP elements and the alpha subunits of RNA polymerase. However, the concurrent up-regulation activity of stress genes by Spx, but not the inhibition of translation related genes, was essential for mediating stress response and antibiotic tolerance under the applied stress conditions. The observed inhibitory activity might be compensated in vivo by additional stress response processes interfering with translation. Nevertheless, the impact of Spx on limiting translation becomes apparent under conditions with high cellular Spx levels. Interestingly, we observed a subpopulation of stationary phase cells that contains raised Spx levels, which may contribute to growth inhibition and a persister-like behaviour of this subpopulation during outgrowth.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Spx, the central regulator of the heat and oxidative stress response in B. subtilis, can repress transcription of translation‐related genes

Schäfer

Heinz

Sudzinová

et al. 2018

Molecular Microbiology

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“…These chaperones either recognize unstructured peptide sequence tags (known as degrons) within a client protein or adaptor proteins bound to target substrates. ClpC exclusively uses adaptor proteins (MecA, YpbH, and McsB) to recognize substrate as well as to promote the activation of the ClpC hexamer [ 38 – 41 ]. Although ClpXP is capable of degrading UgtP in vitro (Fig.…”

Section: Discussionmentioning

confidence: 99%

A nutrient-dependent division antagonist is regulated post-translationally by the Clp proteases in Bacillus subtilis

et al. 2018

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BackgroundChanges in nutrient availability have dramatic and well-defined impacts on both transcription and translation in bacterial cells. At the same time, the role of post-translational control in adaptation to nutrient-poor environments is poorly understood. Previous studies demonstrate the ability of the glucosyltransferase UgtP to influence cell size in response to nutrient availability. Under nutrient-rich medium, interactions with its substrate UDP-glucose promote interactions between UgtP and the tubulin-like cell division protein FtsZ in Bacillus subtilis, inhibiting maturation of the cytokinetic ring and increasing cell size. In nutrient-poor medium, reductions in UDP-glucose availability favor UgtP oligomerization, sequestering it from FtsZ and allowing division to occur at a smaller cell mass.ResultsIntriguingly, in nutrient-poor conditions UgtP levels are reduced ~ 3-fold independent of UDP-glucose. B. subtilis cells cultured under different nutrient conditions indicate that UgtP accumulation is controlled through a nutrient-dependent post-translational mechanism dependent on the Clp proteases. Notably, all three B. subtilis Clp chaperones appeared able to target UgtP for degradation during growth in nutrient-poor conditions.ConclusionsTogether these findings highlight conditional proteolysis as a mechanism for bacterial adaptation to a rapidly changing nutritional landscape.Electronic supplementary materialThe online version of this article (10.1186/s12866-018-1155-2) contains supplementary material, which is available to authorized users.

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“…Bacillus spp. is soil dwelling, aerobic, endospore-forming gram positive rodshaped organism, urease, catalase, gelatin liquefaction positive, while gas, indole, methyl red negative [5]. Bacillus spp are classified as GRAS (Generally Regarded as Safe), and they are safely applied as food ingredients as well as probiotics [6].…”

Section: Isolation and Characterization Of Natural Protease Producersmentioning

confidence: 99%

Isolation and characterization of natural protease producers of Bacillus spp. from Soil samples

Baliu¹,

Hyseni²,

Hyseni³

et al. 2018

2018 UBT International Conference

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Proteases are group of enzymes catalyzing the hydrolysis of proteins. Proteases are considered as commercially most significant among industrial enzymes with wide range of applications in several industries like food, detergent, textile, pulp and paper, and pharmaceutics. Enzymes can be produced by plants, animals or microorganisms, the latter being the dominant host, typically with modified features via recombinant DNA technology for high enzyme production. However, for e.g. food industry, the use of genetically modified microorganisms is not preferred, therefore isolation of new, wild-type microorganism for enzyme production is highly desired. Here we present the results of screening, isolation and characterization of new Bacillus spp. for protease production from soil samples from different areas in Kosovo. Soil samples were divided into four different groups according to their origin: (i) isolates from areas polluted by heavy industry, (ii) isolates from high altitude, (iii) loess sample near thermal water springs, and (iv) arable land. Strains with better protease activity, when compared to the reference strain is obtained.

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Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis

Cited by 43 publications

References 172 publications

Spx, the central regulator of the heat and oxidative stress response in B. subtilis, can repress transcription of translation‐related genes

Spx, the central regulator of the heat and oxidative stress response in B. subtilis, can repress transcription of translation‐related genes

A nutrient-dependent division antagonist is regulated post-translationally by the Clp proteases in Bacillus subtilis

Isolation and characterization of natural protease producers of Bacillus spp. from Soil samples

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