Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4

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Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4. / Feys, Bart J.; Moisan, Lisa J.; Newman, Mari Anne; Parker, Jane E.

I: EMBO Journal, Bind 20, Nr. 19, 01.10.2001, s. 5400-5411.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Feys, BJ, Moisan, LJ, Newman, MA & Parker, JE 2001, 'Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4', EMBO Journal, bind 20, nr. 19, s. 5400-5411. https://doi.org/10.1093/emboj/20.19.5400

APA

Feys, B. J., Moisan, L. J., Newman, M. A., & Parker, J. E. (2001). Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4. EMBO Journal, 20(19), 5400-5411. https://doi.org/10.1093/emboj/20.19.5400

Vancouver

Feys BJ, Moisan LJ, Newman MA, Parker JE. Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4. EMBO Journal. 2001 okt. 1;20(19):5400-5411. https://doi.org/10.1093/emboj/20.19.5400

Author

Feys, Bart J. ; Moisan, Lisa J. ; Newman, Mari Anne ; Parker, Jane E. / Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4. I: EMBO Journal. 2001 ; Bind 20, Nr. 19. s. 5400-5411.

Bibtex

@article{cecb251b598540c2af1788ee5c815ea5,
title = "Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4",
abstract = "The Arabidopsis EDS1 and PAD4 genes encode lipase-like proteins that function in resistance (R) gene-mediated and basal plant disease resistance. Phenotypic analysis of eds1 and pad4 null mutants shows that EDS1 and PAD4 are required for resistance conditioned by the same spectrum of R genes but fulfil distinct roles within the defence pathway. EDS1 is essential for elaboration of the plant hypersensitive response, whereas EDS1 and PAD4 are both required for accumulation of the plant defence-potentiating molecule, salicylic acid. EDS1 is necessary for pathogen-induced PAD4 mRNA accumulation, whereas mutations in PAD4 or depletion of salicylic acid only partially compromise EDS1 expression. Yeast two-hybrid analysis reveals that EDS1 can dimerize and interact with PAD4. However, EDS1 dimerization is mediated by different domains to those involved in EDS1-PAD4 association. Co-immunoprecipitation experiments show that EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells. We propose two functions for EDS1. The first is required early in plant defence, independently of PAD4. The second recruits PAD4 in the amplification of defences, possibly by direct EDS1-PAD4 association.",
keywords = "Arabidopsis, Dimerization, EDS1, PAD4, Salicylic acid",
author = "Feys, {Bart J.} and Moisan, {Lisa J.} and Newman, {Mari Anne} and Parker, {Jane E.}",
year = "2001",
month = oct,
day = "1",
doi = "10.1093/emboj/20.19.5400",
language = "English",
volume = "20",
pages = "5400--5411",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "19",

}

RIS

TY - JOUR

T1 - Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4

AU - Feys, Bart J.

AU - Moisan, Lisa J.

AU - Newman, Mari Anne

AU - Parker, Jane E.

PY - 2001/10/1

Y1 - 2001/10/1

N2 - The Arabidopsis EDS1 and PAD4 genes encode lipase-like proteins that function in resistance (R) gene-mediated and basal plant disease resistance. Phenotypic analysis of eds1 and pad4 null mutants shows that EDS1 and PAD4 are required for resistance conditioned by the same spectrum of R genes but fulfil distinct roles within the defence pathway. EDS1 is essential for elaboration of the plant hypersensitive response, whereas EDS1 and PAD4 are both required for accumulation of the plant defence-potentiating molecule, salicylic acid. EDS1 is necessary for pathogen-induced PAD4 mRNA accumulation, whereas mutations in PAD4 or depletion of salicylic acid only partially compromise EDS1 expression. Yeast two-hybrid analysis reveals that EDS1 can dimerize and interact with PAD4. However, EDS1 dimerization is mediated by different domains to those involved in EDS1-PAD4 association. Co-immunoprecipitation experiments show that EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells. We propose two functions for EDS1. The first is required early in plant defence, independently of PAD4. The second recruits PAD4 in the amplification of defences, possibly by direct EDS1-PAD4 association.

AB - The Arabidopsis EDS1 and PAD4 genes encode lipase-like proteins that function in resistance (R) gene-mediated and basal plant disease resistance. Phenotypic analysis of eds1 and pad4 null mutants shows that EDS1 and PAD4 are required for resistance conditioned by the same spectrum of R genes but fulfil distinct roles within the defence pathway. EDS1 is essential for elaboration of the plant hypersensitive response, whereas EDS1 and PAD4 are both required for accumulation of the plant defence-potentiating molecule, salicylic acid. EDS1 is necessary for pathogen-induced PAD4 mRNA accumulation, whereas mutations in PAD4 or depletion of salicylic acid only partially compromise EDS1 expression. Yeast two-hybrid analysis reveals that EDS1 can dimerize and interact with PAD4. However, EDS1 dimerization is mediated by different domains to those involved in EDS1-PAD4 association. Co-immunoprecipitation experiments show that EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells. We propose two functions for EDS1. The first is required early in plant defence, independently of PAD4. The second recruits PAD4 in the amplification of defences, possibly by direct EDS1-PAD4 association.

KW - Arabidopsis

KW - Dimerization

KW - EDS1

KW - PAD4

KW - Salicylic acid

UR - http://www.scopus.com/inward/record.url?scp=0035477801&partnerID=8YFLogxK

U2 - 10.1093/emboj/20.19.5400

DO - 10.1093/emboj/20.19.5400

M3 - Journal article

C2 - 11574472

AN - SCOPUS:0035477801

VL - 20

SP - 5400

EP - 5411

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 19

ER -

ID: 380058897