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Pathogen-induced protein secretion i...

Cheng, Fang-yi.

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Pathogen-induced protein secretion in plants.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Pathogen-induced protein secretion in plants./
作者:	Cheng, Fang-yi.
面頁冊數:	191 p.
附註:	Source: Dissertation Abstracts International, Volume: 70-01, Section: B, page: 0033.
Contained By:	Dissertation Abstracts International70-01B.
標題:	Biology, Botany. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3345344
ISBN:	9781109005868

Pathogen-induced protein secretion in plants.
Cheng, Fang-yi.

Pathogen-induced protein secretion in plants. - 191 p.

Source: Dissertation Abstracts International, Volume: 70-01, Section: B, page: 0033.

Thesis (Ph.D.)--North Carolina State University, 2008.

The sugar alcohol mannitol is an important carbohydrate in many plants and fungi that has well-documented roles in both metabolism and osmoprotection. In addition, mannitol is an antioxidant, and as such might play a role in host-pathogen interactions. Research suggests that pathogenic fungi secrete mannitol into the plant cell wall to suppress reactive oxygen-mediated host defenses. Previous work suggests that plants counter this by synthesizing the enzyme mannitol dehydrogenase (MTD) to catabolize fungal mannitol. Here we show that the normally cytoplasmic enzyme MTD is exported into the extracellular space in response to the endogenous inducer of plant defense responses, salicylic acid (SA). This SA-induced secretion is resistant to brefeldin A, an inhibitor of Golgi-mediated protein transport. Together with the absence of MTD in Golgi stacks and the lack of a documented extracellular targeting sequence in MTD, this suggests the secretion of MTD is by a non-Golgi, pathogen-activated protein secretion mechanism in plants.

ISBN: 9781109005868Subjects--Topical Terms:

1017825
Biology, Botany.

Pathogen-induced protein secretion in plants.
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245 1 0 $a Pathogen-induced protein secretion in plants.
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500 $a Source: Dissertation Abstracts International, Volume: 70-01, Section: B, page: 0033.
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520 $a The sugar alcohol mannitol is an important carbohydrate in many plants and fungi that has well-documented roles in both metabolism and osmoprotection. In addition, mannitol is an antioxidant, and as such might play a role in host-pathogen interactions. Research suggests that pathogenic fungi secrete mannitol into the plant cell wall to suppress reactive oxygen-mediated host defenses. Previous work suggests that plants counter this by synthesizing the enzyme mannitol dehydrogenase (MTD) to catabolize fungal mannitol. Here we show that the normally cytoplasmic enzyme MTD is exported into the extracellular space in response to the endogenous inducer of plant defense responses, salicylic acid (SA). This SA-induced secretion is resistant to brefeldin A, an inhibitor of Golgi-mediated protein transport. Together with the absence of MTD in Golgi stacks and the lack of a documented extracellular targeting sequence in MTD, this suggests the secretion of MTD is by a non-Golgi, pathogen-activated protein secretion mechanism in plants.
520 $a To further characterize pathogen-activated protein secretion in plants, a comprehensive analysis was performed using Arabidopsis suspension culture to study temporal changes in the cell wall proteome in response to different levels of SA. An LC/MSE label-free proteomic approach was used for simultaneous protein identification and absolute quantification. A total of 76 secreted proteins were identified, 66 of which showed differential secretion patterns in response to SA. A majority of induced protein secretion was observed within the first two hours after treatment, suggesting that many proteins are involved in the early stage of plant defense response. A number of proteins that lacked the signal peptides were detected, indicating that as in many non-plant systems, alternative Golgi/ER-independent secretion mechanisms might exist in plants. Overall, our results provide new and useful insight into plant apoplastic defense mechanisms, and they demonstrate that LC/MS E is a suitable strategy for absolute quantitative proteomic analysis that can be applied to complex experimental designs.
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