Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Evansella cellulosilytica DSM 2522

ABSTRACT: Cellulase producing strain

PROVIDER: PRJNA38423 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR033651.fastq.gz	Fastqsanger.gz
	SRR033652.fastq.gz	Fastqsanger.gz
	SRR033653.fastq.gz	Fastqsanger.gz
	SRR097520.fastq.gz	Fastqsanger.gz
	SRR097521.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 14

Similar Datasets

Xylanimonas cellulosilytica

Project description:Cellulase producing bacterium

| PRJNA60913 | ENA

Evansella cellulosilytica

Project description:An alikiphilic Bacillus

| PRJNA38427 | ENA

The putative cellodextrin transporter-like protein CLP1 is involved in cellulase induction in Neurospora crassa

Project description:Neurospora crassa recently has become a novel system to investigate cellulase induction. Here, we discovered a novel membrane protein, CLP1 (NCU05853), a putative cellodextrin transporter-like protein, that is a critical component of the cellulase induction pathway in N. crassa. Although CLP1 protein cannot transport cellodextrin, the suppression of cellulase induction by this protein was discovered on both cellobiose and Avicel. The co-disruption of the cellodextrin transporters cdt2 and clp1 in strain Δ3βG formed strain CPL7. With induction by cellobiose, cellulase production was enhanced 6.9-fold in CPL7 compared with Δ3βG. We also showed that the suppression of cellulase expression by CLP1 occurred by repressing the expression of cellodextrin transporters, particularly cdt1 expression. Transcriptome analysis of the hypercellulase-producing strain CPL7 showed that the cellulase expression machinery was dramatically stimulated, as were the cellulase enzyme genes including the inducer transporters and the major transcriptional regulators.

2014-11-13 | GSE60004 | GEO

The putative cellodextrin transporter-like protein CLP1 is involved in cellulase induction in Neurospora crassa

Project description:Neurospora crassa recently has become a novel system to investigate cellulase induction. Here, we discovered a novel membrane protein, CLP1 (NCU05853), a putative cellodextrin transporter-like protein, that is a critical component of the cellulase induction pathway in N. crassa. Although CLP1 protein cannot transport cellodextrin, the suppression of cellulase induction by this protein was discovered on both cellobiose and Avicel. The co-disruption of the cellodextrin transporters cdt2 and clp1 in strain M-NM-^T3M-NM-2G formed strain CPL7. With induction by cellobiose, cellulase production was enhanced 6.9-fold in CPL7 compared with M-NM-^T3M-NM-2G. We also showed that the suppression of cellulase expression by CLP1 occurred by repressing the expression of cellodextrin transporters, particularly cdt1 expression. Transcriptome analysis of the hypercellulase-producing strain CPL7 showed that the cellulase expression machinery was dramatically stimulated, as were the cellulase enzyme genes including the inducer transporters and the major transcriptional regulators. N. crassa was pregrown in sucrose and transferred to cellobiose media. Up regulated and down regulated genes expressions were compared with M-NM-^T3M-NM-2G and M-NM-^T3M-NM-2GM-NM-^Tclp1 strain.

2014-11-13 | E-GEOD-60004 | biostudies-arrayexpress

Disruption of serine/threonine protein kinase STK-12 increases cellulase expression in Neurospora crassa

Project description:In this work, we reported that STK-12 functions as a novel repressor of cellulase expression. The stk-12 disruption strain not only displayed enhanced cellulase production but also retained a steady state, with high expression levels of cellulase genes, for longer than the wild type strain.

2022-03-05 | GSE129410 | GEO

Genome sequencing and transcriptome analysis of Trichoderma reesei QM9978 reveals vib1 to be essential for cellulase induction

Project description:The ascomycete Trichoderma reesei is an industrial producer of cellulolytic and hemicellulolytic enzymes and also serves as a model for investigations on these enzymes and their genes. The strain QM9978 has a cellulase negative phenotype and therefore presents a valuable tool for understanding the mechanisms underlying cellulase regulation. A transcriptomic analyses of the cellulase negative strain QM9978 and the original strain QM6a have been performed to identify the genetic differences between QM6a and QM9978 leading to the cellulase-negative phenotype

2017-09-15 | GSE89199 | GEO

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

Transcription factor CrzA modulate fungal development and cellulolytic gene expression in Penicillium oxalicum

Project description:The goals of this study are to compare different gene expressions for Penicillium oxalicum wild type strain (WT), CrzA deletion strain (ΔCrzA) and CrzA recover strain (ReCrzA) in 2% starch as carbon sources. The correlation analysis results between the various samples showed that the gene expression levels of the wild strain and the RecrzA strain were similar, and the gene expression levels between ΔcrzA and the wild strain were significantly different. The deletion of CrzA significantly down-regulates the expression levels of conidia pigment synthesis genes, and spore wall synthesis-related genes of Penicillium oxalicum, and also has a regulatory effect on the expression levels of genes related to the sporulation process. And the absence of CrzA can broadly down-regulate the expression level of cellulase-encoding genes, indicating that CrzA can cause a decrease in cellulase synthesis by affecting the expression of cellulase-encoding genes. The information provided by this study indicates that CrzA function is necessary for the mycelial development and cellulase activity of Penicillium oxalicum.

2021-05-29 | GSE175771 | GEO

The F-box protein Fbx23 regulates the development of Penicillium oxalicum fungi and the expression of cellulolytic genes

Project description:The goals of this study are to compare different gene expressions for Penicillium oxalicum wild type strain (WT), Fbx23 deletion strain (Δfbx23), and Fbx23 ecover strain (Refbx23) under conditions of 2% glucose or 1% bran + 1% microcrystalline cellulose as carbon source. The results of correlation analysis between each sample showed that the gene expression level of Δfbx23 was significantly different from that of the WT strain. The deletion of Fbx23 significantly down-regulates the expression levels of sporulation process genes. And the absence of Fbx23 can broadly up-regulate the expression level of cellulase-encoding genes, indicating that Fbx23 can cause a decrease in cellulase synthesis by affecting the expression of cellulase-encoding genes.

2023-04-03 | GSE228483 | GEO

FaiR regulates the development of Penicillium oxalicum fungi and the expression of cellulolytic genes

Project description:The goals of this study are to compare different gene expressions for Penicillium oxalicum wild type strain (WT) and FaiR deletion strain (DfaiR) under conditions of 1% bran + 1% microcrystalline cellulose as carbon source. The results of correlation analysis between each sample showed that the gene expression level of DfaiR was significantly different from that of the WT strain. The deletion of DfaiR significantly down-regulates the expression levels of sporulation process genes. And the absence of DfaiR can broadly up-regulate the expression level of cellulase-encoding genes, indicating that DfaiR can cause a decrease in cellulase synthesis by affecting the expression of cellulase-encoding genes.

2024-03-13 | GSE261111 | 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