Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors

Citation
Sc. Peck et al., Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors, PL CELL, 13(6), 2001, pp. 1467-1475
Citations number
36
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
PLANT CELL
ISSN journal
1040-4651 → ACNP
Volume
13
Issue
6
Year of publication
2001
Pages
1467 - 1475
Database
ISI
SICI code
1040-4651(200106)13:6<1467:DPIAPP>2.0.ZU;2-5
Abstract
The perception of microbial signal molecules is part of the strategy evolve d by plants to survive attacks by potential pathogens. To gain a more compl ete understanding of the early signaling events involved in these responses , we used radioactive orthophosphate to pulse-label suspension-cultured cel ls of Arabidopsis in conjunction with two-dimensional gel electrophoresis a nd mass spectrometry to identify proteins that are phosphorylated rapidly i n response to bacterial and fungal elicitors. One of these proteins, AtPhos 43, and related proteins in tomato and rice, are phosphorylated within minu tes after treatment with flagellin or chitin fragments. By measuring P-32 i ncorporation into AtPhos43 immunoprecipitated from extracts of elicitor-tre ated hormone and defense-response mutants, we found that phosphorylation of AtPhos43 after flagellin treatment but not chitin treatment is dependent o n FLS2, a receptor-like kinase involved in flagellin perception. Induction by both elicitors is not dependent on salicylic acid or EDS1, a putative li pase involved in defense signaling.