TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity-Reference-Cited by-同舟云学术

TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity

Published:2022-07-29 Issue:6605 Volume:377 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Jia Aolin¹^ORCID,Huang Shijia¹^ORCID,Song Wen²³^ORCID,Wang Junli³^ORCID,Meng Yonggang⁴^ORCID,Sun Yue¹^ORCID,Xu Lina⁵^ORCID,Laessle Henriette³^ORCID,Jirschitzka Jan²³^ORCID,Hou Jiao⁶^ORCID,Zhang Tiantian⁶^ORCID,Yu Wenquan⁶^ORCID,Hessler Giuliana³^ORCID,Li Ertong²^ORCID,Ma Shoucai¹^ORCID,Yu Dongli²³^ORCID,Gebauer Jan²^ORCID,Baumann Ulrich²^ORCID,Liu Xiaohui⁵^ORCID,Han Zhifu¹^ORCID,Chang Junbiao⁴⁶⁷^ORCID,Parker Jane E.³^ORCID,Chai Jijie¹²³^ORCID

Affiliation:

1. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, Center for Plant Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.

2. Institute of Biochemistry, University of Cologne, 50674 Cologne, Germany.

3. Department of Plant-Microbe Interactions, Max-Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.

4. School of Pharmaceutical Sciences, Zhengzhou University, 450001 Zhengzhou, China.

5. National Protein Science Facility, Tsinghua University, 100084 Beijing, China.

6. College of Chemistry, Zhengzhou University, 450001 Zhengzhou, China.

7. Henan Key Laboratory of Organic Functional Molecules and Drug Innovation, Henan Normal University, 453007 Xinxiang, China.

Abstract

Plant pathogen–activated immune signaling by nucleotide-binding leucine-rich repeat (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain converges on Enhanced Disease Susceptibility 1 (EDS1) and its direct partners, Phytoalexin Deficient 4 (PAD4) or Senescence-Associated Gene 101 (SAG101). TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) produces signaling molecules to promote exclusive EDS1-PAD4 and EDS1-SAG101 interactions with helper NLR subclasses. In this work, we show that TIR-containing proteins catalyze adenosine diphosphate (ADP)–ribosylation of adenosine triphosphate (ATP) and ADP ribose (ADPR) through ADPR polymerase–like and NADase activity, forming ADP-ribosylated ATP (ADPr-ATP) and ADPr-ADPR (di-ADPR), respectively. Specific binding of ADPr-ATP or di-ADPR allosterically promotes EDS1-SAG101 interaction with helper NLR N requirement gene 1A (NRG1A) in vitro and in planta. Our data reveal an enzymatic activity of TIRs that enables specific activation of the EDS1-SAG101-NRG1 immunity branch.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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