Effect of clp1 induction on b-dependent gene regulation
Ontology highlight
ABSTRACT:
ORGANISM(S): Mycosarcoma maydis
PROVIDER: GSE21119 | GEO | 2011/03/30
SECONDARY ACCESSION(S): PRJNA126475
REPOSITORIES: GEO
Similar Datasets
Project description:The clp1 gene is a b-regulated gene that is required for clamp formation during the biotrophic growth phase of U. maydis. Clp1 expression blocks b-dependent filament formation and cell cycle arrest if co-induced with the b-heterodimer. Strains AB33 (control) and UMS84 were grown for the times indicated in array medium containing 3 g/l nitrate and 1% arabinose for the induction of nar1P- (bE1/bW2) and crg1P- (clp1) controlled gene expression. Samples were taken from two biological replicates each.
2011-03-30 | E-GEOD-21119 | biostudies-arrayexpress
Project description:The clp1 gene is a b-dependent gene required for clamp formation during the biotrophic growth phase of U. maydis. The gene was induced by means of a fusion to the arabinose inducable crg1 promoter. To exclude effects from the b-mating type locus, the experiments were performed in strain JB1 carrying a deletion of the entire b-locus. Keywords: gene induction
2006-04-25 | GSE4689 | GEO
Project description:The clp1 gene is a b-regulated gene that is required for clamp formation during the biotrophic growth phase of U. maydis. Interaction studies demonstrated that Clp1 imnteracts with Rbf1, the central regulator of pathogenciity. To exclude b-dependent effects the experiments were performed in a b-null background to analyze clp1-depndent effects on rbf controlled gene regulation
2010-09-17 | GSE21121 | GEO
Project description:The clp1 gene is a b-regulated gene that is required for clamp formation during the biotrophic growth phase of U. maydis. Interaction studies demonstrated that Clp1 imnteracts with Rbf1, the central regulator of pathogenciity. To exclude b-dependent effects the experiments were performed in a b-null background to analyze clp1-depndent effects on rbf controlled gene regulation Strains UKH156 (nitrate inducible Rbf1 expression) and UKH164 (arabinose-inducible Clp1 and and nitrate-inducible Rbf1 expression) were grown for 12h in liquid array medium/nitrate/arabinose.
2010-09-17 | E-GEOD-21121 | biostudies-arrayexpress
Project description:Ustilago maydis strain JB1 was modified to include an arabinose inducible clp1 in the ip-locus and clb1 was deleted.
2019-04-04 | E-MTAB-7463 | biostudies-arrayexpress
Project description:The biotrophic fungal pathogen Ustilago maydis cause common smut in maize, and lead to gall formation on all aerial organs, especially on maize kernel thus reduce yield. The interaction of U. maydis with maize is a well-established model to study the interaction between maize and biotrophic pathogen. U. maydis infection could activate host immune responses including: ROS accumulation, protease activation, salicylic acid signaling. U. maydis employ several strategies to overcome maize immune response, thus initial the biotrophic interaction with host. It has been suggested that genetic factors of maize host affected the disease severity of U. maydis infection, here we investigated the transcriptome profile of resistance and susceptible maize lines upon U. maydis infection, thus propose candidate maize genes involved in the defense response in maize to corn smut cause by U. maydis.
2021-04-15 | GSE172071 | GEO
Project description:RNAseq of Ustilago maydis with inducible clp1 and Δcib1
| PRJEB30058 | ENA
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
Project description:CLP1 was the first mammalian RNA kinase to be identified. However, determining its in vivo function has been elusive. Here we generated kinase-dead Clp1 (Clp1K/K) mice that show a progressive loss of spinal motor neurons associated with axonal degeneration in the peripheral nerves and denervation of neuromuscular junctions, resulting in impaired motor function, muscle weakness, paralysis and fatal respiratory failure. Transgenic rescue experiments show that CLP1 functions in motor neurons. Mechanistically, loss of CLP1 activity results in accumulation of a novel set of small RNA fragments, derived from aberrant processing of tyrosine pre-transfer RNA. These tRNA fragments sensitize cells to oxidative-stress-induced p53 (also known as TRP53) activation and p53-dependent cell death. Genetic inactivation of p53 rescues Clp1K/K mice from the motor neuron loss, muscle denervation and respiratory failure. Our experiments uncover a mechanistic link between tRNA processing, formation of a new RNA species and progressive loss of lower motor neurons regulated by p53.
2013-03-12 | GSE35924 | GEO
Project description:CLP1 was the first mammalian RNA kinase to be identified. However, determining its in vivo function has been elusive. Here we generated kinase-dead Clp1 (Clp1K/K) mice that show a progressive loss of spinal motor neurons associated with axonal degeneration in the peripheral nerves and denervation of neuromuscular junctions, resulting in impaired motor function, muscle weakness, paralysis and fatal respiratory failure. Transgenic rescue experiments show that CLP1 functions in motor neurons. Mechanistically, loss of CLP1 activity results in accumulation of a novel set of small RNA fragments, derived from aberrant processing of tyrosine pre-transfer RNA. These tRNA fragments sensitize cells to oxidative-stress-induced p53 (also known as TRP53) activation and p53-dependent cell death. Genetic inactivation of p53 rescues Clp1K/K mice from the motor neuron loss, muscle denervation and respiratory failure. Our experiments uncover a mechanistic link between tRNA processing, formation of a new RNA species and progressive loss of lower motor neurons regulated by p53. RNA was extracted from spinal cord of 3 Clp1 knock-out mice and 3 wild type mice (15 days old, male, all samples age and sex matched) and submitted to differential splicing analysis using Affymetrix Exon microarrays. Differential splicing analysis was performed between the Clp1 KO and WT samles employing a custom CDF, that was based on a complete re-alignment of oligonucleotide probes to the genome and transcriptome (Ensembl 52, ASTD 1.1; further information on http://bioinfo.i-med.ac.at).
2013-03-12 | E-GEOD-35924 | biostudies-arrayexpress