Global and local gene expression in rice leaves and roots challenged by Magnaporthe oryzae
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ABSTRACT:
ORGANISM(S): Oryza sativa
PROVIDER: GSE62896 | GEO | 2015/02/20
SECONDARY ACCESSION(S): PRJNA265992
REPOSITORIES: GEO
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Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
2015-02-20 | E-GEOD-62896 | biostudies-arrayexpress
Project description:This SuperSeries is composed of the SubSeries listed below.
2009-04-08 | GSE8670 | GEO
Project description:Somatic embryogenesis receptor kinase (SERK) proteins play pivotal roles in regulation of plant development and immunity. The rice genome contains two SERK genes, OsSerk1 and OsSerk2. We previously demonstrated that OsSerk2 is required for rice Xa21-mediated resistance to Xanthomonas oryzae pv. oryzae (Xoo) and for normal development. Here we report the molecular characterization of OsSerk1. Overexpression of OsSerk1 results in a semi-dwarf phenotype whereas silencing of OsSerk1 results in a reduced angle of the lamina joint. OsSerk1 is not required for rice resistance to Xoo or Magnaporthe oryzae. Overexpression of OsSerk1 in OsSerk2-silenced lines complements phenotypes associated with brassinosteroid (BR) signaling defects, but not the disease resistance phenotype mediated by Xa21. In yeast, OsSERK1 interacts with itself forming homodimers, and also interacts with the kinase domains of OsSERK2 and BRI1, respectively. OsSERK1 is a functional protein kinase capable of auto-phosphorylation in vitro. We conclude that, whereas OsSERK2 regulates both rice development and immunity, OsSERK1 functions in rice development but not immunity to Xoo and M. oryzae.
| S-EPMC4253019 | biostudies-literature
Project description:BackgroundThe annual yield losses caused by the Rice Blast Fungus, Magnaporthe oryzae, range to the equivalent for feeding 60 million people. To ward off infection by this fungus, rice has evolved a generic basal immunity (so called compatible interaction), which acts in concert with strain-specific defence (so-called incompatible interaction). The plant-defence hormone jasmonic acid (JA) promotes the resistance to M. oryzae, but the underlying mechanisms remain elusive. To get more insight into this open question, we employ the JA-deficient mutants, cpm2 and hebiba, and dissect the JA-dependent defence signalling in rice for both, compatible and incompatible interactions.ResultsWe observe that both JA-deficient mutants are more susceptible to M. oryzae as compared to their wild-type background, which holds true for both types of interactions as verified by cytological staining. Secondly, we observe that transcripts for JA biosynthesis (OsAOS2 and OsOPR7), JA signalling (OsJAZ8, OsJAZ9, OsJAZ11 and OsJAZ13), JA-dependent phytoalexin synthesis (OsNOMT), and JA-regulated defence-related genes, such as OsBBTI2 and OsPR1a, accumulate after fungal infection in a pattern that correlates with the amplitude of resistance. Thirdly, induction of defence transcripts is weaker during compatible interaction.ConclusionThe study demonstrates the pivotal role of JA in basal immunity of rice in the resistance to M. oryzae in both, compatible and incompatible interactions.
| S-EPMC9764487 | biostudies-literature
Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
2012-12-07 | E-GEOD-36785 | biostudies-arrayexpress
Project description:This SuperSeries is composed of the SubSeries listed below.
2012-12-07 | GSE36785 | GEO
Project description:The exocyst, an evolutionarily conserved octameric protein complex, mediates tethering of vesicles to the plasma membrane in the early stage of exocytosis. Arabidopsis Exo70, a subunit of the exocyst complex, has been found to be involved in plant immunity. Here, we characterize the function of OsExo70B1 in rice. OsExo70B1 mainly expresses in leaf and shoot and its expression is induced by pathogen-associated molecular patterns (PAMPs) and rice blast fungus Magnaporthe oryzae (M. oryzae). Knocking out OsExo70B1 results in significantly decreased resistance and defense responses to M. oryzae compared to the wild type, including more disease lesions and enhanced fungal growth, downregulated expression of pathogenesis-related (PR) genes, and decreased reactive oxygen species accumulation. In contrast, the exo70B1 mutant does not show any defects in growth and development. Furthermore, OsExo70B1 can interact with the receptor-like kinase OsCERK1, an essential component for chitin reception in rice. Taken together, our data demonstrate that OsExo70B1 functions as an important regulator in rice immunity.
| S-EPMC7582735 | biostudies-literature
Project description:Magnaporthe oryzae (M. oryzae) is a fungal pathogen and the causal agent of rice blast disease. Previous lipidomics analysis of M. oryzae demonstrated that trehalose, a carbohydrate common to various fungi and algae, is thought to be involved in the possible conversion of glycogen into triacylglycerides for energy, an important step in the pathogenesis of M. oryzae. A key enzyme responsible for trehalose synthesis is trehalose-6-phosphate synthase 1 (Tps1). Therefore, we modeled the structure of Tps1 and sought to screen a chemical database in silico for possible inhibitors of the enzyme. Based on homologous alignment and sequence analysis, we first modeled the structure of Tps1 to determine the potential active site of the enzyme and its conformation. Using this model, we then undertook a docking study to determine the potential interaction that would manifest between Tsp1 and potential chemical inhibitors. Of the 400,000 chemicals screened in the Molecular Libraries Small Molecule Repository, we identified 45 potential candidates. The best candidate (Compound 24789937) was chosen and subjected to various structural optimization techniques to improve the suitability of the potential chemical inhibitors at the docking site of Tps1. From these modified versions of Compound 24789937, one lead compound (Lead 25) was shown to have the best binding affinity to Tps1 and good water solubility as compared with the ideal template compound and the other 44 potential candidates. Molecular dynamics simulation further confirmed the strength of the Tps1-Lead 25 complex and indicated the potential for Lead 25 to be used as an inhibitor of Tps1 in the control of M. oryzae-mediated rice blast disease.
| S-EPMC3901853 | biostudies-literature
Project description:BackgroundMagnaporthe oryzae, the causal agent of blast disease of rice, is the most destructive disease of rice worldwide. The genome of this fungal pathogen has been sequenced and an automated annotation has recently been updated to Version 6 http://www.broad.mit.edu/annotation/genome/magnaporthe_grisea/MultiDownloads.html. However, a comprehensive manual curation remains to be performed. Gene Ontology (GO) annotation is a valuable means of assigning functional information using standardized vocabulary. We report an overview of the GO annotation for Version 5 of M. oryzae genome assembly.MethodsA similarity-based (i.e., computational) GO annotation with manual review was conducted, which was then integrated with a literature-based GO annotation with computational assistance. For similarity-based GO annotation a stringent reciprocal best hits method was used to identify similarity between predicted proteins of M. oryzae and GO proteins from multiple organisms with published associations to GO terms. Significant alignment pairs were manually reviewed. Functional assignments were further cross-validated with manually reviewed data, conserved domains, or data determined by wet lab experiments. Additionally, biological appropriateness of the functional assignments was manually checked.ResultsIn total, 6,286 proteins received GO term assignment via the homology-based annotation, including 2,870 hypothetical proteins. Literature-based experimental evidence, such as microarray, MPSS, T-DNA insertion mutation, or gene knockout mutation, resulted in 2,810 proteins being annotated with GO terms. Of these, 1,673 proteins were annotated with new terms developed for Plant-Associated Microbe Gene Ontology (PAMGO). In addition, 67 experiment-determined secreted proteins were annotated with PAMGO terms. Integration of the two data sets resulted in 7,412 proteins (57%) being annotated with 1,957 distinct and specific GO terms. Unannotated proteins were assigned to the 3 root terms. The Version 5 GO annotation is publically queryable via the GO site http://amigo.geneontology.org/cgi-bin/amigo/go.cgi. Additionally, the genome of M. oryzae is constantly being refined and updated as new information is incorporated. For the latest GO annotation of Version 6 genome, please visit our website http://scotland.fgl.ncsu.edu/smeng/GoAnnotationMagnaporthegrisea.html. The preliminary GO annotation of Version 6 genome is placed at a local MySql database that is publically queryable via a user-friendly interface Adhoc Query System.ConclusionOur analysis provides comprehensive and robust GO annotations of the M. oryzae genome assemblies that will be solid foundations for further functional interrogation of M. oryzae.
| S-EPMC2654668 | biostudies-literature
Project description:This SuperSeries is composed of the SubSeries listed below.
2023-11-29 | GSE246679 | GEO