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Induction of CtsR-regulated chaperones improves Xylanase production in Bacillus subtilis

ABSTRACT: Induction of CtsR-regulated chaperones improves Xylanase production in Bacillus subtilis

PROVIDER: PRJNA901390 | ENA |

REPOSITORIES: ENA

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Induction of CtsR-regulated chaperones improves Xylanase production in Bacillus subtilis

Project description:We examined the effect of high-level expression of the commercially important endo-1,4-β-xylanase XynA on the B. subtilis transcriptome using RNA-seq. Rather unexpectedly, we found a reduced expression of several protein chaperones, including ClpC, ClpE and ClpX, was downregulated when XynA was overproduced. Expression of these proteins is controlled by the transcriptional repressor CtsR. CtsR levels are directly controlled by regulated proteolysis, involving ClpC and its cognate protease ClpP. Preventing this downregulation by knocking out the involved transcriptional repressor CtsR resulted in increased XynA production by more than 25 %.

2023-02-21 | GSE217916 | GEO

Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis

Project description:In a previous study we used RNA-seq to identify cellular stresses related to the overexpression of xylanase XynA, and found that upregulation of the CtsR regulon improves the yield of XynA production in B. subtilis. In this study, we compared the transcriptomes of B. subtilis cells overexpressing either the xylanase XynA or the heterologous amylase AmyM, to identify general and enzyme-specific stress responses. In addition, we further compared the translational profiles of cells overexpressing XynA and AmyM using ribosome profiling.

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Comparative genomic, transcriptomic and secretomic profilings of Penicillium oxalicum HP7-1 and its cellulase and xylanase hyper-producing mutant EU2106, and identification of two novel regulators for cellulase and xylanase gene expression

Project description:In this study,comparative genomic, transcriptomic and secretomic profilings of Penicillium oxalicum HP7-1 and its cellulase and xylanase hyper-producing mutant EU2106 were employed to screen for novel regulators for cellulase and xylanase gene expression.

2016-08-31 | GSE80076 | GEO

Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis

Project description:Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis

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Effects of transcription factor POX04513 on the transcription of cellulase genes and xylanase genes in Penicillium oxalicum

Project description:To investigate the effect of the transcription factor POX04513 in Penicillium oxalicum on the expression levels of cellulase and xylanase genes in solid and liquid fermentation

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Large-scale transcriptomic analyses reveal a global co-expression network of cellulase and xylanase genes in filamentous fungi

Project description:A global co-expression network of cellulase and xylanase genes was identified in P. oxalicum, their transcriptional levels depended on the induction of carbon sources and induction time.

2020-04-27 | GSE133258 | GEO

Prokaryotic expression profiling analysis for single or combined chaperones deletion

Project description:Chaperones have essential role in assist nascent peptides folding, prevent proteins aggregation and maintain cellular protein homeostasis. Considering spatial and temporal features of chaperones regulating in vivo, changes in single or combined chaperone-depleted E.coli strain is needed to be put into understand at transcriptional level. Here, we utilized expression microarrays to investigate global transcriptional response upon deletion of single or multiple chaperones in E. coli for understanding the transcriptional network affected by chaperones. To identify prokaryotic expression profiles in deletion of chaperones, several E.coli mutants were constructed in the following: Z116 (△tig 37℃), Z125(△dnaK37℃), Z625(△tig△dnaK 37℃ or 30℃), Z629(△tig△dnaK 30℃), NM (C-domain of tig was deleted 37℃), MC (N-domain of tig was deleted 37℃), NC (M-domain of tig was deleted 37℃). Two types of cDNA mixtures containing Cy3-labeled (or Cy5-labeled) control DNA (from BW25113) and Cy5-labeled (or Cy3-labeled) DNA targets (from mutant strain) were hybridized with E.coli microarrays in a dye-swap strategy.

2015-06-18 | GSE69912 | GEO

Prokaryotic expression profiling analysis for single or combined chaperones deletion

2015-06-18 | E-GEOD-69912 | biostudies-arrayexpress

Host chaperones can define the fitness of adaptive influenza variants

Project description:The threat of viral pandemics demands a comprehensive understanding of evolution at the host-pathogen interface. Here, we systematically show that the accessibility of adaptive mutations in influenza nucleoprotein at fever-like temperatures is mediated by host chaperones. Particularly noteworthy, we observe that the Pro283 nucleoprotein variant, which is conserved across human flu strains, confers resistance to the MxA antiviral-restriction factor, and critically contributed to the pathogenicity of the 1918 pandemic flu, is rendered unfit by host chaperone depletion. This fitness loss is linked to biophysical defects that chaperones cannot address when heat shock factor-I is inhibited. Thus, host chaperones can be hijacked by viruses to un-couple biophysically deleterious consequences of mutations from the benefits of immune escape. In summary, host chaperones play a central role in shaping influenza adaptation, with implications for the evolution of other viruses, for viral host-switching, and for the design of antiviral strategies refractory to resistance.

2018-09-10 | GSE113649 | GEO

Inhibition of extracellular proteases improves the production of a xylanase in Parageobacillus thermoglucosidasius.

Project description:BACKGROUND:Parageobacillus thermoglucosidasius is a thermophilic and ethanol-producing bacterium capable of utilising both hexose and pentose sugars for fermentation. The organism has been proposed to be a suitable organism for the production of bioethanol from lignocellulosic feedstocks. These feedstocks may be difficult to degrade, and a potential strategy to optimise this process is to engineer strains that secrete hydrolases that liberate increased amounts of sugars from those feedstocks. However, very little is known about protein transport in P. thermoglucosidasius and the limitations of that process, and as a first step we investigated whether there were bottlenecks in the secretion of a model protein. RESULTS:A secretory enzyme, xylanase (XynA1), was produced with and without its signal peptide. Cell cultures were fractionated into cytoplasm, membrane, cell wall, and extracellular milieu protein extracts, which were analysed using immunoblotting and enzyme activity assays. The main bottleneck identified was proteolytic degradation of XynA1 during or after its translocation. A combination of mass spectrometry and bioinformatics indicated the presence of several proteases that might be involved in this process. CONCLUSION:The creation of protease-deficient strains may be beneficial towards the development of P. thermoglucosidasius as a platform organism for industrial processes.

| S-EPMC6425571 | biostudies-literature

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