The Arabidopsis PAD4 Lipase-Like Domain Is Sufficient for Resistance to Green Peach Aphid
Plants have evolved mechanisms to protect themselves against pathogenic microbes and insect pests. In , the immune regulator PAD4 functions with its cognate partner EDS1 to limit pathogen growth. PAD4, independently of EDS1, reduces infestation by green peach aphid (GPA). How PAD4 regulates these de...
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Veröffentlicht in: | Molecular plant-microbe interactions 2020-02, Vol.33 (2), p.328-335 |
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container_title | Molecular plant-microbe interactions |
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creator | Dongus, Joram A Bhandari, Deepak D Patel, Monika Archer, Lani Dijkgraaf, Lucas Deslandes, Laurent Shah, Jyoti Parker, Jane E |
description | Plants have evolved mechanisms to protect themselves against pathogenic microbes and insect pests. In
, the immune regulator PAD4 functions with its cognate partner EDS1 to limit pathogen growth. PAD4, independently of EDS1, reduces infestation by green peach aphid (GPA). How PAD4 regulates these defense outputs is unclear. By expressing the N-terminal PAD4 lipase-like domain (PAD4
) without its C-terminal EDS1-PAD4 (EP) domain, we interrogated PAD4 functions in plant defense. Here, we show that transgenic expression of PAD4
in
is sufficient for limiting GPA infestation but not for conferring basal and effector-triggered pathogen immunity. This suggests that the C-terminal PAD4 EP domain is necessary for EDS1-dependent immune functions but is dispensable for aphid resistance. Moreover, PAD4
is not sufficient to interact with EDS1, indicating the PAD4-EP domain is required for stable heterodimerization. These data provide molecular evidence that PAD4 has domain-specific functions. |
doi_str_mv | 10.1094/MPMI-08-19-0245-R |
format | Article |
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, the immune regulator PAD4 functions with its cognate partner EDS1 to limit pathogen growth. PAD4, independently of EDS1, reduces infestation by green peach aphid (GPA). How PAD4 regulates these defense outputs is unclear. By expressing the N-terminal PAD4 lipase-like domain (PAD4
) without its C-terminal EDS1-PAD4 (EP) domain, we interrogated PAD4 functions in plant defense. Here, we show that transgenic expression of PAD4
in
is sufficient for limiting GPA infestation but not for conferring basal and effector-triggered pathogen immunity. This suggests that the C-terminal PAD4 EP domain is necessary for EDS1-dependent immune functions but is dispensable for aphid resistance. Moreover, PAD4
is not sufficient to interact with EDS1, indicating the PAD4-EP domain is required for stable heterodimerization. These data provide molecular evidence that PAD4 has domain-specific functions.</description><identifier>ISSN: 0894-0282</identifier><identifier>EISSN: 1943-7706</identifier><identifier>DOI: 10.1094/MPMI-08-19-0245-R</identifier><identifier>PMID: 31702436</identifier><language>eng</language><publisher>United States: American Phytopathological Society</publisher><subject>Animals ; Aphids - physiology ; Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis - parasitology ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Carboxylic Ester Hydrolases - genetics ; Carboxylic Ester Hydrolases - metabolism ; Disease Resistance - genetics ; Gene Expression Regulation, Plant ; Infestation ; Insects ; Life Sciences ; Lipase ; Pathogens ; Pest resistance ; Pests ; Phytopathology and phytopharmacy ; Plant protection ; Protein Domains - genetics ; Protein Domains - physiology ; Transgenic plants ; Vegetal Biology</subject><ispartof>Molecular plant-microbe interactions, 2020-02, Vol.33 (2), p.328-335</ispartof><rights>Copyright American Phytopathological Society Feb 2020</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-f7696698098b2de139d7e1c233b97004c5e41ab680ae69495f38c6003f42b113</citedby><cites>FETCH-LOGICAL-c406t-f7696698098b2de139d7e1c233b97004c5e41ab680ae69495f38c6003f42b113</cites><orcidid>0000-0002-8553-6802 ; 0000-0002-4700-6480 ; 0000-0003-1974-5144</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31702436$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://cnrs.hal.science/hal-02409700$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Dongus, Joram A</creatorcontrib><creatorcontrib>Bhandari, Deepak D</creatorcontrib><creatorcontrib>Patel, Monika</creatorcontrib><creatorcontrib>Archer, Lani</creatorcontrib><creatorcontrib>Dijkgraaf, Lucas</creatorcontrib><creatorcontrib>Deslandes, Laurent</creatorcontrib><creatorcontrib>Shah, Jyoti</creatorcontrib><creatorcontrib>Parker, Jane E</creatorcontrib><title>The Arabidopsis PAD4 Lipase-Like Domain Is Sufficient for Resistance to Green Peach Aphid</title><title>Molecular plant-microbe interactions</title><addtitle>Mol Plant Microbe Interact</addtitle><description>Plants have evolved mechanisms to protect themselves against pathogenic microbes and insect pests. In
, the immune regulator PAD4 functions with its cognate partner EDS1 to limit pathogen growth. PAD4, independently of EDS1, reduces infestation by green peach aphid (GPA). How PAD4 regulates these defense outputs is unclear. By expressing the N-terminal PAD4 lipase-like domain (PAD4
) without its C-terminal EDS1-PAD4 (EP) domain, we interrogated PAD4 functions in plant defense. Here, we show that transgenic expression of PAD4
in
is sufficient for limiting GPA infestation but not for conferring basal and effector-triggered pathogen immunity. This suggests that the C-terminal PAD4 EP domain is necessary for EDS1-dependent immune functions but is dispensable for aphid resistance. Moreover, PAD4
is not sufficient to interact with EDS1, indicating the PAD4-EP domain is required for stable heterodimerization. These data provide molecular evidence that PAD4 has domain-specific functions.</description><subject>Animals</subject><subject>Aphids - physiology</subject><subject>Arabidopsis</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - parasitology</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Carboxylic Ester Hydrolases - genetics</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Disease Resistance - genetics</subject><subject>Gene Expression Regulation, Plant</subject><subject>Infestation</subject><subject>Insects</subject><subject>Life Sciences</subject><subject>Lipase</subject><subject>Pathogens</subject><subject>Pest resistance</subject><subject>Pests</subject><subject>Phytopathology and phytopharmacy</subject><subject>Plant protection</subject><subject>Protein Domains - genetics</subject><subject>Protein Domains - physiology</subject><subject>Transgenic plants</subject><subject>Vegetal Biology</subject><issn>0894-0282</issn><issn>1943-7706</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUFv1DAQhS0EotvCD-CCLHGhh9Bx7Dj2MWppu1Kqrpa9cLIcZ6J12Y2DnSDx70m0bQ-cRpr53tM8PUI-MfjGQIurh83DOgOVMZ1BLops-4asmBY8K0uQb8kKlBbzReVn5DylJwCmZVG8J2eclbOAyxX5udsjraJtfBuG5BPdVDeC1n6wCbPa_0J6E47W93Sd6I-p67zz2I-0C5FuceZH2zukY6B3EbGnG7RuT6th79sP5F1nDwk_Ps8Lsrv9vru-z-rHu_V1VWdOgByzrpRaSq1AqyZvkXHdlshcznmjSwDhChTMNlKBRamFLjqunATgncgbxvgFuTzZ7u3BDNEfbfxrgvXmvqrNspuDwuL0Z2G_ntghht8TptEcfXJ4ONgew5RMzhnnpWRSzOiX_9CnMMV-DjJTRQ4lKMVnip0oF0NKEbvXDxiYpSKzVGRAGaaXRwqznTWfn52n5ojtq-KlE_4P1ZSILQ</recordid><startdate>20200201</startdate><enddate>20200201</enddate><creator>Dongus, Joram A</creator><creator>Bhandari, Deepak D</creator><creator>Patel, Monika</creator><creator>Archer, Lani</creator><creator>Dijkgraaf, Lucas</creator><creator>Deslandes, Laurent</creator><creator>Shah, Jyoti</creator><creator>Parker, Jane E</creator><general>American Phytopathological Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>K9.</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-8553-6802</orcidid><orcidid>https://orcid.org/0000-0002-4700-6480</orcidid><orcidid>https://orcid.org/0000-0003-1974-5144</orcidid></search><sort><creationdate>20200201</creationdate><title>The Arabidopsis PAD4 Lipase-Like Domain Is Sufficient for Resistance to Green Peach Aphid</title><author>Dongus, Joram A ; 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In
, the immune regulator PAD4 functions with its cognate partner EDS1 to limit pathogen growth. PAD4, independently of EDS1, reduces infestation by green peach aphid (GPA). How PAD4 regulates these defense outputs is unclear. By expressing the N-terminal PAD4 lipase-like domain (PAD4
) without its C-terminal EDS1-PAD4 (EP) domain, we interrogated PAD4 functions in plant defense. Here, we show that transgenic expression of PAD4
in
is sufficient for limiting GPA infestation but not for conferring basal and effector-triggered pathogen immunity. This suggests that the C-terminal PAD4 EP domain is necessary for EDS1-dependent immune functions but is dispensable for aphid resistance. Moreover, PAD4
is not sufficient to interact with EDS1, indicating the PAD4-EP domain is required for stable heterodimerization. These data provide molecular evidence that PAD4 has domain-specific functions.</abstract><cop>United States</cop><pub>American Phytopathological Society</pub><pmid>31702436</pmid><doi>10.1094/MPMI-08-19-0245-R</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-8553-6802</orcidid><orcidid>https://orcid.org/0000-0002-4700-6480</orcidid><orcidid>https://orcid.org/0000-0003-1974-5144</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Animals Aphids - physiology Arabidopsis Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - parasitology Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Carboxylic Ester Hydrolases - genetics Carboxylic Ester Hydrolases - metabolism Disease Resistance - genetics Gene Expression Regulation, Plant Infestation Insects Life Sciences Lipase Pathogens Pest resistance Pests Phytopathology and phytopharmacy Plant protection Protein Domains - genetics Protein Domains - physiology Transgenic plants Vegetal Biology |
title | The Arabidopsis PAD4 Lipase-Like Domain Is Sufficient for Resistance to Green Peach Aphid |
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