Loading…
Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight
Most characterized plant resistance proteins belong to the nucleotide-binding domain and Leu-rich repeat-containing (NLR) family. NLRs are present in an auto-inhibited state in the absence of specific pathogens, while gain-of-function mutations in NLRs usually cause autoimmunity. Here, we show that...
Saved in:
Published in: | Plant physiology (Bethesda) 2019-11, Vol.181 (3), p.1295-1313 |
---|---|
Main Authors: | , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c326t-77c9466a14f4f925b83a00f6d5deb70aab3368f48e2911ad45db462a19f468df3 |
---|---|
cites | |
container_end_page | 1313 |
container_issue | 3 |
container_start_page | 1295 |
container_title | Plant physiology (Bethesda) |
container_volume | 181 |
creator | Tang, Jiuyou Wang, Yiqin Yin, Wenchao Dong, Guojun Sun, Kai Teng, Zhenfeng Wu, Xujiang Wang, Shimei Qian, Yangwen Pan, Xuebiao Qian, Qian Chu, Chengcai |
description | Most characterized plant resistance proteins belong to the nucleotide-binding domain and Leu-rich repeat-containing (NLR) family. NLRs are present in an auto-inhibited state in the absence of specific pathogens, while gain-of-function mutations in NLRs usually cause autoimmunity. Here, we show that a gain-of-function mutation,
(
), which caused a Phe-to-Leu substitution in the nucleotide-binding domain of a typical NLR in rice (
), led to enhanced susceptibility to
pv.
The unexpected accumulation of salicylic acid (SA), along with downregulation of
(
), in
indicates the potential presence of a feedback regulation loop of SA biosynthesis in rice. Epistasis analyses illustrated that SA accumulation and the NLR-associated components RAR1, OsRac1, and PhyB are dispensable for the
phenotypes. Intriguingly, besides pattern-triggered immunity, effector-triggered immunity conferred by different resistance proteins, including Xa3/Xa26, Xa4, and Xa21, was also disturbed by
to a certain extent, indicating the existence of shared regulatory mechanisms for various defense systems. The identification of
therefore provides a unique system for genetic dissection of shared immune signaling pathways activated by different types of immune receptors. |
doi_str_mv | 10.1104/pp.19.00686 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2312274413</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2312274413</sourcerecordid><originalsourceid>FETCH-LOGICAL-c326t-77c9466a14f4f925b83a00f6d5deb70aab3368f48e2911ad45db462a19f468df3</originalsourceid><addsrcrecordid>eNo9kEFP3DAQha0KVBboqXfkI1KVxWM73uTYhZYiLbRaLefIccZglMSu7Qjtv2_apVzevJE-vcNHyGdgSwAmr0JYQr1kTFXqA1lAKXjBS1kdkQVjc2dVVZ-Q05ReGGMgQH4kJ3MKKIEvyOv9lHV2fqTeUk0fJtOjz67DYu3Gzo1PdIOTcSMWW2ee6RYD6kzvhmEacf4MhuxjsdsHpL-iz-hGeuNSnEJOB8rlPc2errXJGJ3u6bp3T8_5nBxb3Sf89HbPyOP3b7vrH8Xm5-3d9ddNYQRXuVitTC2V0iCttDUv20poxqzqyg7bFdO6FUJVVlbIawDdybJrpeIaaitV1VlxRi4PuyH63xOm3AwuGex7PaKfUsMFcL6SEsSMfjmgJvqUItomRDfouG-ANX9NNyE0UDf_TM_0xdvw1A7YvbP_1Yo_8Tp55g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2312274413</pqid></control><display><type>article</type><title>Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight</title><source>Oxford Journals Online</source><creator>Tang, Jiuyou ; Wang, Yiqin ; Yin, Wenchao ; Dong, Guojun ; Sun, Kai ; Teng, Zhenfeng ; Wu, Xujiang ; Wang, Shimei ; Qian, Yangwen ; Pan, Xuebiao ; Qian, Qian ; Chu, Chengcai</creator><creatorcontrib>Tang, Jiuyou ; Wang, Yiqin ; Yin, Wenchao ; Dong, Guojun ; Sun, Kai ; Teng, Zhenfeng ; Wu, Xujiang ; Wang, Shimei ; Qian, Yangwen ; Pan, Xuebiao ; Qian, Qian ; Chu, Chengcai</creatorcontrib><description>Most characterized plant resistance proteins belong to the nucleotide-binding domain and Leu-rich repeat-containing (NLR) family. NLRs are present in an auto-inhibited state in the absence of specific pathogens, while gain-of-function mutations in NLRs usually cause autoimmunity. Here, we show that a gain-of-function mutation,
(
), which caused a Phe-to-Leu substitution in the nucleotide-binding domain of a typical NLR in rice (
), led to enhanced susceptibility to
pv.
The unexpected accumulation of salicylic acid (SA), along with downregulation of
(
), in
indicates the potential presence of a feedback regulation loop of SA biosynthesis in rice. Epistasis analyses illustrated that SA accumulation and the NLR-associated components RAR1, OsRac1, and PhyB are dispensable for the
phenotypes. Intriguingly, besides pattern-triggered immunity, effector-triggered immunity conferred by different resistance proteins, including Xa3/Xa26, Xa4, and Xa21, was also disturbed by
to a certain extent, indicating the existence of shared regulatory mechanisms for various defense systems. The identification of
therefore provides a unique system for genetic dissection of shared immune signaling pathways activated by different types of immune receptors.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.19.00686</identifier><identifier>PMID: 31431512</identifier><language>eng</language><publisher>United States</publisher><subject>Gene Expression Regulation, Plant - genetics ; Leucine-Rich Repeat Proteins ; Mutation - genetics ; Oryza - genetics ; Oryza - metabolism ; Oryza - microbiology ; Plant Diseases - microbiology ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Proteins - genetics ; Proteins - metabolism ; Xanthomonas - pathogenicity</subject><ispartof>Plant physiology (Bethesda), 2019-11, Vol.181 (3), p.1295-1313</ispartof><rights>2019 American Society of Plant Biologists. All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c326t-77c9466a14f4f925b83a00f6d5deb70aab3368f48e2911ad45db462a19f468df3</citedby><orcidid>0000-0002-7556-4404 ; 0000-0002-7062-3495 ; 0000-0003-4517-8139 ; 0000-0002-9059-2139 ; 0000-0002-0349-4937 ; 0000-0001-8097-6115</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31431512$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tang, Jiuyou</creatorcontrib><creatorcontrib>Wang, Yiqin</creatorcontrib><creatorcontrib>Yin, Wenchao</creatorcontrib><creatorcontrib>Dong, Guojun</creatorcontrib><creatorcontrib>Sun, Kai</creatorcontrib><creatorcontrib>Teng, Zhenfeng</creatorcontrib><creatorcontrib>Wu, Xujiang</creatorcontrib><creatorcontrib>Wang, Shimei</creatorcontrib><creatorcontrib>Qian, Yangwen</creatorcontrib><creatorcontrib>Pan, Xuebiao</creatorcontrib><creatorcontrib>Qian, Qian</creatorcontrib><creatorcontrib>Chu, Chengcai</creatorcontrib><title>Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Most characterized plant resistance proteins belong to the nucleotide-binding domain and Leu-rich repeat-containing (NLR) family. NLRs are present in an auto-inhibited state in the absence of specific pathogens, while gain-of-function mutations in NLRs usually cause autoimmunity. Here, we show that a gain-of-function mutation,
(
), which caused a Phe-to-Leu substitution in the nucleotide-binding domain of a typical NLR in rice (
), led to enhanced susceptibility to
pv.
The unexpected accumulation of salicylic acid (SA), along with downregulation of
(
), in
indicates the potential presence of a feedback regulation loop of SA biosynthesis in rice. Epistasis analyses illustrated that SA accumulation and the NLR-associated components RAR1, OsRac1, and PhyB are dispensable for the
phenotypes. Intriguingly, besides pattern-triggered immunity, effector-triggered immunity conferred by different resistance proteins, including Xa3/Xa26, Xa4, and Xa21, was also disturbed by
to a certain extent, indicating the existence of shared regulatory mechanisms for various defense systems. The identification of
therefore provides a unique system for genetic dissection of shared immune signaling pathways activated by different types of immune receptors.</description><subject>Gene Expression Regulation, Plant - genetics</subject><subject>Leucine-Rich Repeat Proteins</subject><subject>Mutation - genetics</subject><subject>Oryza - genetics</subject><subject>Oryza - metabolism</subject><subject>Oryza - microbiology</subject><subject>Plant Diseases - microbiology</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Xanthomonas - pathogenicity</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNo9kEFP3DAQha0KVBboqXfkI1KVxWM73uTYhZYiLbRaLefIccZglMSu7Qjtv2_apVzevJE-vcNHyGdgSwAmr0JYQr1kTFXqA1lAKXjBS1kdkQVjc2dVVZ-Q05ReGGMgQH4kJ3MKKIEvyOv9lHV2fqTeUk0fJtOjz67DYu3Gzo1PdIOTcSMWW2ee6RYD6kzvhmEacf4MhuxjsdsHpL-iz-hGeuNSnEJOB8rlPc2errXJGJ3u6bp3T8_5nBxb3Sf89HbPyOP3b7vrH8Xm5-3d9ddNYQRXuVitTC2V0iCttDUv20poxqzqyg7bFdO6FUJVVlbIawDdybJrpeIaaitV1VlxRi4PuyH63xOm3AwuGex7PaKfUsMFcL6SEsSMfjmgJvqUItomRDfouG-ANX9NNyE0UDf_TM_0xdvw1A7YvbP_1Yo_8Tp55g</recordid><startdate>201911</startdate><enddate>201911</enddate><creator>Tang, Jiuyou</creator><creator>Wang, Yiqin</creator><creator>Yin, Wenchao</creator><creator>Dong, Guojun</creator><creator>Sun, Kai</creator><creator>Teng, Zhenfeng</creator><creator>Wu, Xujiang</creator><creator>Wang, Shimei</creator><creator>Qian, Yangwen</creator><creator>Pan, Xuebiao</creator><creator>Qian, Qian</creator><creator>Chu, Chengcai</creator><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>7X8</scope><orcidid>https://orcid.org/0000-0002-7556-4404</orcidid><orcidid>https://orcid.org/0000-0002-7062-3495</orcidid><orcidid>https://orcid.org/0000-0003-4517-8139</orcidid><orcidid>https://orcid.org/0000-0002-9059-2139</orcidid><orcidid>https://orcid.org/0000-0002-0349-4937</orcidid><orcidid>https://orcid.org/0000-0001-8097-6115</orcidid></search><sort><creationdate>201911</creationdate><title>Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight</title><author>Tang, Jiuyou ; Wang, Yiqin ; Yin, Wenchao ; Dong, Guojun ; Sun, Kai ; Teng, Zhenfeng ; Wu, Xujiang ; Wang, Shimei ; Qian, Yangwen ; Pan, Xuebiao ; Qian, Qian ; Chu, Chengcai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-77c9466a14f4f925b83a00f6d5deb70aab3368f48e2911ad45db462a19f468df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Gene Expression Regulation, Plant - genetics</topic><topic>Leucine-Rich Repeat Proteins</topic><topic>Mutation - genetics</topic><topic>Oryza - genetics</topic><topic>Oryza - metabolism</topic><topic>Oryza - microbiology</topic><topic>Plant Diseases - microbiology</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Xanthomonas - pathogenicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tang, Jiuyou</creatorcontrib><creatorcontrib>Wang, Yiqin</creatorcontrib><creatorcontrib>Yin, Wenchao</creatorcontrib><creatorcontrib>Dong, Guojun</creatorcontrib><creatorcontrib>Sun, Kai</creatorcontrib><creatorcontrib>Teng, Zhenfeng</creatorcontrib><creatorcontrib>Wu, Xujiang</creatorcontrib><creatorcontrib>Wang, Shimei</creatorcontrib><creatorcontrib>Qian, Yangwen</creatorcontrib><creatorcontrib>Pan, Xuebiao</creatorcontrib><creatorcontrib>Qian, Qian</creatorcontrib><creatorcontrib>Chu, Chengcai</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tang, Jiuyou</au><au>Wang, Yiqin</au><au>Yin, Wenchao</au><au>Dong, Guojun</au><au>Sun, Kai</au><au>Teng, Zhenfeng</au><au>Wu, Xujiang</au><au>Wang, Shimei</au><au>Qian, Yangwen</au><au>Pan, Xuebiao</au><au>Qian, Qian</au><au>Chu, Chengcai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2019-11</date><risdate>2019</risdate><volume>181</volume><issue>3</issue><spage>1295</spage><epage>1313</epage><pages>1295-1313</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>Most characterized plant resistance proteins belong to the nucleotide-binding domain and Leu-rich repeat-containing (NLR) family. NLRs are present in an auto-inhibited state in the absence of specific pathogens, while gain-of-function mutations in NLRs usually cause autoimmunity. Here, we show that a gain-of-function mutation,
(
), which caused a Phe-to-Leu substitution in the nucleotide-binding domain of a typical NLR in rice (
), led to enhanced susceptibility to
pv.
The unexpected accumulation of salicylic acid (SA), along with downregulation of
(
), in
indicates the potential presence of a feedback regulation loop of SA biosynthesis in rice. Epistasis analyses illustrated that SA accumulation and the NLR-associated components RAR1, OsRac1, and PhyB are dispensable for the
phenotypes. Intriguingly, besides pattern-triggered immunity, effector-triggered immunity conferred by different resistance proteins, including Xa3/Xa26, Xa4, and Xa21, was also disturbed by
to a certain extent, indicating the existence of shared regulatory mechanisms for various defense systems. The identification of
therefore provides a unique system for genetic dissection of shared immune signaling pathways activated by different types of immune receptors.</abstract><cop>United States</cop><pmid>31431512</pmid><doi>10.1104/pp.19.00686</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0002-7556-4404</orcidid><orcidid>https://orcid.org/0000-0002-7062-3495</orcidid><orcidid>https://orcid.org/0000-0003-4517-8139</orcidid><orcidid>https://orcid.org/0000-0002-9059-2139</orcidid><orcidid>https://orcid.org/0000-0002-0349-4937</orcidid><orcidid>https://orcid.org/0000-0001-8097-6115</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0032-0889 |
ispartof | Plant physiology (Bethesda), 2019-11, Vol.181 (3), p.1295-1313 |
issn | 0032-0889 1532-2548 |
language | eng |
recordid | cdi_proquest_miscellaneous_2312274413 |
source | Oxford Journals Online |
subjects | Gene Expression Regulation, Plant - genetics Leucine-Rich Repeat Proteins Mutation - genetics Oryza - genetics Oryza - metabolism Oryza - microbiology Plant Diseases - microbiology Plant Proteins - genetics Plant Proteins - metabolism Proteins - genetics Proteins - metabolism Xanthomonas - pathogenicity |
title | Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T05%3A59%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Mutation%20of%20a%20Nucleotide-Binding%20Leucine-Rich%20Repeat%20Immune%20Receptor-Type%20Protein%20Disrupts%20Immunity%20to%20Bacterial%20Blight&rft.jtitle=Plant%20physiology%20(Bethesda)&rft.au=Tang,%20Jiuyou&rft.date=2019-11&rft.volume=181&rft.issue=3&rft.spage=1295&rft.epage=1313&rft.pages=1295-1313&rft.issn=0032-0889&rft.eissn=1532-2548&rft_id=info:doi/10.1104/pp.19.00686&rft_dat=%3Cproquest_cross%3E2312274413%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c326t-77c9466a14f4f925b83a00f6d5deb70aab3368f48e2911ad45db462a19f468df3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2312274413&rft_id=info:pmid/31431512&rfr_iscdi=true |