Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR22273579.fastq.gz	Fastqsanger.gz
	SRR22273580.fastq.gz	Fastqsanger.gz
	SRR22273581.fastq.gz	Fastqsanger.gz
	SRR22273582.fastq.gz	Fastqsanger.gz
	SRR22273583.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 8

Similar Datasets

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.

2024-08-30 | GSE270692 | GEO

Induction of the CtsR regulon improves Xylanase production in Bacillus subtilis.

Project description:BackgroundThe bacterium Bacillus subtilis is extensively used for the commercial production of enzymes due to its efficient protein secretion capacity. However, the efficiency of secretion varies greatly between enzymes, and despite many years of research, optimization of enzyme production is still largely a matter of trial-and-error. Genome-wide transcriptome analysis seems a useful tool to identify relevant secretion bottlenecks, yet to this day, only a limited number of transcriptome studies have been published that focus on enzyme secretion in B. subtilis. Here, we examined the effect of high-level expression of the commercially important enzyme endo-1,4-β-xylanase XynA on the B. subtilis transcriptome using RNA-seq.ResultsUsing the novel gene-set analysis tool GINtool, we found a reduced activity of the CtsR regulon when XynA was overproduced. This regulon comprises several protein chaperone genes, including clpC, clpE and clpX, and is controlled by transcriptional repression. CtsR levels are directly controlled by regulated proteolysis, involving ClpC and its cognate protease ClpP. When we abolished this negative feedback, by inactivating the repressor CtsR, the XynA production increased by 25%.ConclusionsOverproduction of enzymes can reduce the pool of Clp protein chaperones in B. subtilis, presumably due to negative feedback regulation. Breaking this feedback can improve enzyme production yields. Considering the conserved nature of Clp chaperones and their regulation, this method might benefit high-yield enzyme production in other organisms.

| S-EPMC10633939 | biostudies-literature

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

| PRJNA1128008 | ENA

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

2023-05-06 | GSE154882 | GEO

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

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data