Ontology highlight
ABSTRACT:
PROVIDER: PRJNA748763 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR15210400.fastq.gz | Fastqsanger.gz | |||
| SRR15210401.fastq.gz | Fastqsanger.gz | |||
| SRR15210402.fastq.gz | Fastqsanger.gz | |||
| SRR15210403.fastq.gz | Fastqsanger.gz | |||
| SRR15210404.fastq.gz | Fastqsanger.gz |
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Project description:Janthinobacterium rivuli strain:MSP1 Genome sequencing
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Project description:Magnaporthe oryzae snodprot1 homolog (MSP1), a recently identified PAMP, is known to trigger defense responses in rice. However, the receptor(s) and downstream interacting components of MSP1 in rice have not been identified so far. Using multiple immunoprecipitation-mass spectrometry (IP-MS) analyses in transgenic rice expressing MSP1-YFP, we identified several heat shock proteins (HSPs) as MSP1 interacting partners. Heat stress treatment suppressed MSP1-induced cell death in tobacco plants transiently expressing MSP1. Subsequent IP-MS analysis on these tobacco plants, exposed to heat stress, resulted in the identification of a HSP having a highly conserved sequence to the OsHSP70 of rice. Co-expression of MSP1 with OsHSP70 failed to induce cell death in tobacco, confirming the involvement of the OsHSP70 in the MSP1 immune response. Rice protoplasts, co-expressing MSP1 and OsHSP70, showed a direct interaction between these two proteins in planta. Taken together, the results reported here highlight the pivotal role of OsHSP70 in MSP1-induced signaling and enhance our understanding of rice-M. oryzae interaction.
2025-04-23 | PXD057048 | Pride
Project description:MSP1 is a Magnaporthe oryzae secreted protein that elicits defense responses in rice. However, the molecular mechanism of MSP1 action is largely elusive. Here, we employed a TMT-based quantitative proteomic analysis of cytoplasmic as well as plasma membrane proteins to decipher the MSP1 induced signalling in rice. This approach led to the identification of 6691 proteins of which 3049 were identified in the plasma membrane (PM) while 3642 were identified in the cytoplasmic fraction. A parallel phosphoproteome analysis led to the identification of 1906 phosphopeptides and integration of proteome and phosphoproteome data showed activation of proteins related to the proteolysis, jasmonic acid biosynthesis, redox metabolism and MAP kinase signaling pathways in response to MSP1 treatment. Further, MSP1 induced phosphorylation of some of the key proteins including RBOHB, MEKK1, MPK3/6, CDPK and CaM suggest activation of PAMP-triggered immunity (PTI) in response to MSP1 treatment. In essence, our results further support the functioning of MSP1 as a PAMP and provide an overview of the MSP1 induced signaling in rice leaves.
2019-08-30 | PXD014758 | Pride
Project description:Magnaporthe oryzae snodprot1 homologous protein (MSP1) has been shown to act as a pathogen-associated molecular pattern (PAMPs) and trigger PAMP-triggered immunity (PTI) response involving programmed cell death and expression of various defense-related genes in rice. The involvement of several post-translational modifications (PTMs) in the regulation of plant immune response, especially PTI, during pathogen infection is well established, however, the information on the regulatory roles of these PTMs in response to MSP1-induced signaling in rice is currently elusive. Here, we report the phosphoproteome, ubiquitinome, and acetylproteome to investigate the MSP1-induced PTMs alterations in MSP1 overexpressed rice. Our analysis identified a total of 4,666 PTM modified sites in rice leaves including 4,292 phosphosites, 189 ubiquitin sites, and 185 acetylation sites. Among these, PTM status of 437 phosphorylated, 53 ubiquitinated, and 68 acetylated peptides were significantly changed by MSP1. Functional annotation of MSP1 modulated peptides by MapMan analysis revealed that these were majorly associated with cellular immune responses such as signaling, transcription factors, DNA and RNA regulation, and protein metabolism, among others. Taken together, this study uncovers the MSP1-induced PTMs changes in rice proteins and identified several novel components of rice-MSP1 interaction.
2023-07-21 | PXD039997 | Pride
Project description:Pathogen secreted pathogen-associated molecular patterns (PAMPs) play a key role in PAMPs triggered immunity (PTI) in plant for the recognition of pathogens. In rice, fewer PAMPs and their pattern recognition receptors (PRRs) have been characterized during rice-Magnaporthe oryzae interaction. Particularly, recent study was identified M. oryzae snodprot1 homolog known as MSP1, however, the molecular mechanism of MSP1 induced PTI is currently elusive. Therefore, we were generated the MSP1 overexpressed transgenic rice with their subcellular localization in the apoplastic (with signal sequence) and cytoplasmic (without signal sequence) regions, respectively, to examine the functional role of MSP1 in rice. Here, we employed a tandem mass tag (TMT)-based quantitative membrane proteomic analysis to decipher the potential interaction PRRs and MSP1-induced downstream signaling. This approach led to the identification of 8,033 proteins and sequential statistical analysis were identified 2,226 differentially modulated proteins. Of these, 20 plasma membrane localized receptor like kinases (RLKs) with the increased abundance in response to MSP1. Moreover, activation of proteins related to the protein degradation and modification, calcium signaling, transcription factor, redox, and MAPK signaling were characterized. Taken together, our results indicated that potential PRR candidates involved in response to blast disease and thus suggesting the overview mechanism of the MSP1-induced signaling in rice leaves.
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