The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor

Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) in the defense response of Chinese wi...

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Published inThe New phytologist Vol. 200; no. 3; pp. 834 - 846
Main Authors Yu, Yihe, Xu, Weirong, Wang, Jie, Wang, Lei, Yao, Wenkong, Yang, Yazhou, Xu, Yan, Ma, Fuli, Du, Yangjian, Wang, Yuejin
Format Journal Article
LanguageEnglish
Published England New Phytologist Trust 01.11.2013
Wiley Subscription Services, Inc
Subjects
Airborne microorganisms
Amino Acid Sequence
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis - microbiology
Defense mechanisms
defense response
Degradation
Disease resistance
Disease Resistance - genetics
Domains
E3 ubiquitin ligase
Erysiphe necator
Gene Expression Regulation, Plant
Gene regulation
Genes
Genes, Plant
grapevine
Leaves
Molecular Sequence Data
Pathogens
Plant cells
Plant diseases
Plant Diseases - genetics
Plant Diseases - microbiology
Plant immunity
Plant Proteins - genetics
Plant Proteins - metabolism
Plants
Powdery mildew
Proteasome 26S
Proteins
Proteolysis
Pseudomonas syringae
RING Finger Domains
Tomatoes
Transcription
transcription factor
Transcription factors
Transcription Factors - metabolism
Transcription, Genetic
Transgenic plants
Ubiquitin
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - metabolism
Ubiquitins
Vitis - genetics
Vitis - metabolism
Vitis - microbiology
Vitis pseudoreticulata
Yeasts
transcription factor
E3 ubiquitin ligase
Vitis pseudoreticulata
defense response
grapevine
proteolysis
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Abstract Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata. The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4-type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W-box-dependent transcription in planta. EIRP1 targeted VpWRKY11 in vivo, resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome.
AbstractList Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata. The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4-type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W-box-dependent transcription in planta. EIRP1 targeted VpWRKY11 in vivo, resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome.
Summary Ubiquitin‐mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator‐induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata. The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4‐type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W‐box‐dependent transcription in planta. EIRP1 targeted VpWRKY11 in vivo, resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome.
Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata. The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4-type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W-box-dependent transcription in planta. EIRP1 targeted VpWRKY11 in vivo, resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome.
Summary Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata. The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4-type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W-box-dependent transcription in planta. EIRP1 targeted VpWRKY11 in vivo, resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome. [PUBLICATION ABSTRACT]
Summary Ubiquitin‐mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we investigated the role of the E3 ubiquitin ligase Erysiphe necator ‐induced RING finger protein 1 (EIRP1) in the defense response of Chinese wild grapevine Vitis pseudoreticulata . The regulatory function of E3 ubiquitin ligase EIRP1 was investigated using molecular, genetic and biochemical approaches. EIRP1 encodes a C3HC4‐type Really Interesting New Gene (RING) finger protein that harbors E3 ligase activity. This activity requires the conserved RING domain, and VpWRKY11 also interacts with EIRP1 through the RING domain. VpWRKY11 localizes to the nucleus and activates W‐box‐dependent transcription in planta . EIRP1 targeted VpWRKY11 in vivo , resulting in VpWRKY11 degradation. The expression of EIRP1 and VpWRKY11 responds rapidly to powdery mildew in Vitis pseudoreticulata grapevine; also, overexpression of EIRP1 in Arabidopsis confers enhanced resistance to the pathogens Golovinomyces cichoracearum and Pseudomonas syringae pv tomato DC3000. Our data suggest that the EIRP1 E3 ligase positively regulates plant disease resistance by mediating proteolysis of the negative regulator VpWRKY11 via degradation by the 26S proteasome.
Author Yihe Yu
Yazhou Yang
Weirong Xu
Yuejin Wang
Lei Wang
Fuli Ma
Yangjian Du
Jie Wang
Wenkong Yao
Yan Xu
Author_xml – sequence: 1
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  organization: Northwest A&F University
– sequence: 10
  givenname: Yuejin
  surname: Wang
  fullname: Wang, Yuejin
  organization: Northwest A&F University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/23905547$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright 2013 New Phytologist Trust
2013 College of Horticulture. New Phytologist © 2013 New Phytologist Trust
2013 College of Horticulture. New Phytologist © 2013 New Phytologist Trust.
Copyright © 2013 New Phytologist Trust
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– notice: 2013 College of Horticulture. New Phytologist © 2013 New Phytologist Trust.
– notice: Copyright © 2013 New Phytologist Trust
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Issue 3
Keywords transcription factor
E3 ubiquitin ligase
Vitis pseudoreticulata
defense response
grapevine
proteolysis
Language English
License 2013 College of Horticulture. New Phytologist © 2013 New Phytologist Trust.
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Snippet Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we...
Summary Ubiquitin‐mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack....
Summary Ubiquitin-mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack....
Ubiquitin‐mediated regulation responds rapidly to specific stimuli; this rapidity is particularly important for defense responses to pathogen attack. Here, we...
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jstor
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StartPage 834
SubjectTerms Airborne microorganisms
Amino Acid Sequence
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis - microbiology
Defense mechanisms
defense response
Degradation
Disease resistance
Disease Resistance - genetics
Domains
E3 ubiquitin ligase
Erysiphe necator
Gene Expression Regulation, Plant
Gene regulation
Genes
Genes, Plant
grapevine
Leaves
Molecular Sequence Data
Pathogens
Plant cells
Plant diseases
Plant Diseases - genetics
Plant Diseases - microbiology
Plant immunity
Plant Proteins - genetics
Plant Proteins - metabolism
Plants
Powdery mildew
Proteasome 26S
Proteins
Proteolysis
Pseudomonas syringae
RING Finger Domains
Tomatoes
Transcription
transcription factor
Transcription factors
Transcription Factors - metabolism
Transcription, Genetic
Transgenic plants
Ubiquitin
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - metabolism
Ubiquitins
Vitis - genetics
Vitis - metabolism
Vitis - microbiology
Vitis pseudoreticulata
Yeasts
Title The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor
URI https://www.jstor.org/stable/newphytologist.200.3.834
https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fnph.12418
https://www.ncbi.nlm.nih.gov/pubmed/23905547
https://www.proquest.com/docview/1441672309/abstract/
https://www.proquest.com/docview/2513388509/abstract/
https://search.proquest.com/docview/1461336947
Volume 200
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