Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight. Issue 3 (29th August 2019)
- Record Type:
- Journal Article
- Title:
- Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight. Issue 3 (29th August 2019)
- Main Title:
- Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight
- Authors:
- Tang, Jiuyou
Wang, Yiqin
Yin, Wenchao
Dong, Guojun
Sun, Kai
Teng, Zhenfeng
Wu, Xujiang
Wang, Shimei
Qian, Yangwen
Pan, Xuebiao
Qian, Qian
Chu, Chengcai - Abstract:
- Abstract : A gain-of-function mutation in a nucleotide-binding leucine-rich repeat immune receptor-type protein suppresses pattern-triggered or effector-triggered immunity to Xanthomonas oryzae in rice. 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, weaker defense ( wed ), which caused a Phe-to-Leu substitution in the nucleotide-binding domain of a typical NLR in rice ( Oryza sativa ), led to enhanced susceptibility to Xanthomonas oryzae pv. Oryzae . The unexpected accumulation of salicylic acid (SA), along with downregulation of NONEXPRESSOR OF PR1 ( NPR1 ), in wed 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 wed phenotypes. Intriguingly, besides pattern-triggered immunity, effector-triggered immunity conferred by different resistance proteins, including Xa3/Xa26, Xa4, and Xa21, was also disturbed by wed to a certain extent, indicating the existence of shared regulatory mechanisms for various defense systems. The identification of wed therefore provides a unique system for genetic dissection of shared immuneAbstract : A gain-of-function mutation in a nucleotide-binding leucine-rich repeat immune receptor-type protein suppresses pattern-triggered or effector-triggered immunity to Xanthomonas oryzae in rice. 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, weaker defense ( wed ), which caused a Phe-to-Leu substitution in the nucleotide-binding domain of a typical NLR in rice ( Oryza sativa ), led to enhanced susceptibility to Xanthomonas oryzae pv. Oryzae . The unexpected accumulation of salicylic acid (SA), along with downregulation of NONEXPRESSOR OF PR1 ( NPR1 ), in wed 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 wed phenotypes. Intriguingly, besides pattern-triggered immunity, effector-triggered immunity conferred by different resistance proteins, including Xa3/Xa26, Xa4, and Xa21, was also disturbed by wed to a certain extent, indicating the existence of shared regulatory mechanisms for various defense systems. The identification of wed therefore provides a unique system for genetic dissection of shared immune signaling pathways activated by different types of immune receptors. … (more)
- Is Part Of:
- Plant physiology. Volume 181:Issue 3(2019)
- Journal:
- Plant physiology
- Issue:
- Volume 181:Issue 3(2019)
- Issue Display:
- Volume 181, Issue 3 (2019)
- Year:
- 2019
- Volume:
- 181
- Issue:
- 3
- Issue Sort Value:
- 2019-0181-0003-0000
- Page Start:
- 1295
- Page End:
- 1313
- Publication Date:
- 2019-08-29
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.19.00686 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
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- 22688.xml