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231223s2008 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/ern044
|2 doi
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|a pubmed25n0596.xml
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|a (DE-627)NLM178722383
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|a (NLM)18390849
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Rivière, Marie-Pierre
|e verfasserin
|4 aut
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| 245 |
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|a Silencing of acidic pathogenesis-related PR-1 genes increases extracellular beta-(1->3)-glucanase activity at the onset of tobacco defence reactions
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 24.06.2008
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The class 1 pathogenesis-related (PR) proteins are thought to be involved in plant defence responses, but their molecular functions are unknown. The function of PR-1 was investigated in tobacco by generating stable PR-1a-silenced lines in which other acidic PR-1 genes (PR-1b and PR-1c) were silenced. Plants lacking extracellular PR-1s were more susceptible than wild-type plants to the oomycete Phytophthora parasitica but displayed unaffected systemic acquired resistance and developmental resistance to this pathogen. Treatment with salicylic acid up-regulates the PR-1g gene, encoding a basic protein of the PR-1 family, in PR-1-deficient tobacco, indicating that PR-1 expression may repress that of PR-1g. This shows that acidic PR-1s are dispensable for expression of salicylic acid-dependent acquired resistances against P. parasitica and may reveal a functional overlap in tobacco defence or a functional redundancy in the PR-1 gene family. The data also show that there is a specific increase in apoplastic beta-(1-->3)-glucanase activity and a decrease in beta-(1-->3)-glucan deposition in PR-1-silenced lines following activation of defence reactions. Complementation of the silencing by apoplastic treatment with a recombinant PR-1a protein largely restores the wild-type beta-(1-->3)-glucanase activity and callose phenotype. Taken together with the immunolocalization of PR-1a to sites of beta-(1-->3)-glucan deposition in wild-type plants, these results are indicative of a function for PR-1a in regulation of enzymatic activity of extracellular beta-(1-->3)-glucanases
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Algal Proteins
|2 NLM
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|a Fungal Proteins
|2 NLM
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|a Glucans
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Protein Isoforms
|2 NLM
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|a Recombinant Proteins
|2 NLM
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| 650 |
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|a cryptogein protein, Phytophthora cryptogea
|2 NLM
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| 650 |
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|a pathogenesis-related proteins, plant
|2 NLM
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| 650 |
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|a callose
|2 NLM
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| 650 |
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|a 9064-51-1
|2 NLM
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| 650 |
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|a Glucan 1,3-beta-Glucosidase
|2 NLM
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| 650 |
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|a EC 3.2.1.58
|2 NLM
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| 650 |
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|a Salicylic Acid
|2 NLM
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| 650 |
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|a O414PZ4LPZ
|2 NLM
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| 700 |
1 |
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|a Marais, Antoine
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ponchet, Michel
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Willats, William
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Galiana, Eric
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 59(2008), 6 vom: 01., Seite 1225-39
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnas
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| 773 |
1 |
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|g volume:59
|g year:2008
|g number:6
|g day:01
|g pages:1225-39
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/ern044
|3 Volltext
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|d 59
|j 2008
|e 6
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