Proteornics of the response of Arabidopsis thaliana to infection with Alternaria brassicicola

被引:71
|
作者
Mukherjee, Arup K. [2 ]
Carp, Marie-Jeanne
Zuchman, Rina [1 ]
Ziv, Tamar [1 ]
Horwitz, Benjamin A. [1 ]
Gepstein, Shimon
机构
[1] Technion Israel Inst Technol, Dept Biol, Smoler Prote Ctr, IL-32000 Haifa, Israel
[2] Cent Inst Cotton Res, Div Plant Protect, Nagpur, Maharashtra, India
关键词
PLANT-PATHOGEN INTERACTIONS; LEAF SENESCENCE; SALICYLIC-ACID; DEFENSE RESPONSES; SCALE PROTEOMICS; CELL-DEATH; GENE; RESISTANCE; REVEALS; ETHYLENE;
D O I
10.1016/j.jprot.2009.10.005
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
We have studied the proteome of the model plant Arabidopsis thaliana infected with a necrotrophic fungal pathogen, Alternaria brassicicola. The Arabidopsis-A. brassicicola host-pathogen pair is being developed as a model genetic system for incompatible plant-fungal interactions, in which the spread of disease is limited by plant defense responses. After confirming that a defense response was induced at the transcriptional level, we identified proteins whose abundance on 2-DE gels increased or decreased in infected leaves. Atleast 11 protein spots showed reproducible differences in abundance, increasing or decreasing during the progress of the infection. The pathogenesis-related protein PR4, a glycosyl hydrolase, and the antifungal protein osmotin are strongly up-regulated. Two members of the Arabidopsis glutathione S-transferase (GST) family increased in abundance in infected leaves. The spots in which these GST proteins were identified contain additional members of the GST family. Representation of GST family members in several protein spots migrating at similar molecular weight suggests post-translational modifications. The signature of GST regulation may be specific for the type of plant-pathogen interaction. The proteomic view of the defense response to A. brassicicola can be compared with other types of plant-pathogen interactions, and to leaf senescence, identifying unique regulatory patterns. (C) 2009 Elsevier B.V. All rights reserved.
引用
收藏
页码:709 / 720
页数:12
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