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  • Wei, Yuming  (2)
  • Biodiversity Research  (2)
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  • Biodiversity Research  (2)
  • 1
    In: Molecular Plant Pathology, Wiley, Vol. 24, No. 10 ( 2023-10), p. 1205-1219
    Abstract: The dynamic balance and distribution of sphingolipid metabolites modulate the level of programmed cell death and plant defence. However, current knowledge is still limited regarding the molecular mechanism underlying the relationship between sphingolipid metabolism and plant defence. In this study, we identified a wheat RNA‐binding protein 1 (TaRBP1) and TaRBP1 mRNA accumulation significantly decreased in wheat after infection by Puccinia striiformis f . sp. tritici (Pst). Knockdown of TaRBP1 via virus‐induced gene silencing conferred strong resistance to Pst by enhancing host plant reactive oxygen species (ROS) accumulation and cell death, indicating that TaRBP1 may act as a negative regulator in response to Pst. TaRBP1 formed a homopolymer and interacted with TaRBP1 C‐terminus in plants. Additionally, TaRBP1 physically interacted with TaGLTP, a sphingosine transfer protein. Knockdown of TaGLTP enhanced wheat resistance to the virulent Pst CYR31. Sphingolipid metabolites showed a significant accumulation in TaGLTP ‐silenced wheat and TaRBP1 ‐silenced wheat, respectively. In the presence of the TaRBP1 protein, TaGLTP failed to be degraded in a 26S proteasome‐dependent manner in plants. Our results reveal a novel susceptible mechanism by which a plant fine‐tunes its defence responses by stabilizing TaGLTP accumulation to suppress ROS and sphingolipid accumulation during Pst infection.
    Type of Medium: Online Resource
    ISSN: 1464-6722 , 1364-3703
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 2020755-4
    detail.hit.zdb_id: 2010497-2
    SSG: 12
    Location Call Number Limitation Availability
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  • 2
    In: Molecular Plant Pathology, Wiley, Vol. 24, No. 12 ( 2023-12), p. 1495-1509
    Abstract: Chitin is a long‐chain polymer of β‐1,4‐linked N ‐acetylglucosamine that forms rigid microfibrils to maintain the hyphal form and protect it from host attacks. Chitin oligomers are first recognized by the plant receptors in the apoplast region, priming the plant's immune system. Here, seven polysaccharide deacetylases (PDAs) were identified and their activities on chitin substrates were investigated via systematic characterization of the PDA family from Fusarium graminearum . Among these PDAs, FgPDA5 was identified as an important virulence factor and was specifically expressed during pathogenesis. Δ Fgpda5 compromised the pathogen's ability to infect wheat. The polysaccharide deacetylase structure of FgPDA5 is essential for the pathogenicity of F. graminearum . FgPDA5 formed a homodimer and accumulated in the plant apoplast. In addition, FgPDA5 showed a high affinity toward chitin substrates. FgPDA5‐mediated deacetylation of chitin oligomers prevented activation of plant defence responses. Overall, our results identify FgPDA5 as a polysaccharide deacetylase that can prevent chitin‐triggered host immunity in plant apoplast through deacetylation of chitin oligomers.
    Type of Medium: Online Resource
    ISSN: 1464-6722 , 1364-3703
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2023
    detail.hit.zdb_id: 2020755-4
    detail.hit.zdb_id: 2010497-2
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
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