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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  • M.P. Riviere
  • A. Marais
  • M. Ponchet
  • W. Willats
  • E. Galiana
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
Udgivelsesdato: 2008
Original languageEnglish
JournalJournal of Experimental Botany
Volume59
Issue number6
Pages (from-to)1225-1239
Number of pages14
ISSN0022-0957
DOIs
Publication statusPublished - 2008

Bibliographical note

Key words: ARR, callose, ß-(13)-glucanase, PR-1a, RNAi, SAR

ID: 10028119