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From Proteopedia
Cryo-EM structure of EDS1 and SAG101 with ATP-APDR
Structural highlights
Function[EDS1C_ARATH] Positive regulator of basal resistance and of effector-triggered immunity specifically mediated by TIR-NB-LRR (TNL) resistance proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR resistance protein interactions constitutes the first step in resistance activation (PubMed:22158819). Acts redundantly with salicylic acid to regulate resistance gene-mediated signaling (PubMed:19578402). Triggers early plant defenses and hypersensitive response independently of PAD4, and then recruits PAD4 to potentiate plant defenses through the accumulation of salicylic acid (PubMed:11574472). Nuclear localization is essential for basal and TNL-conditioned immunity and for reprogramming defense gene expression, while cytoplasmic EDS1 is required to induce a complete immune response (PubMed:20617163). Heterodimerization with PAD4 and/or SGA101 is necessary for TNL-mediated effector-triggered immunity (PubMed:24331460). Contributes to nonhost resistance against E.amylovora (PubMed:22316300). Loss of EDS1-PAD4 interaction compromises basal but not TNL-triggered resistance (PubMed:21434927). Necessary for systemic acquired resistance (SAR) signal generation and perception (PubMed:24755512). Has no direct lipase activity (PubMed:16040633). Putative lipase activity is dispensable for immune functions (PubMed:24331460).[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedPlant 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. TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity.,Jia A, Huang S, Song W, Wang J, Meng Y, Sun Y, Xu L, Laessle H, Jirschitzka J, Hou J, Zhang T, Yu W, Hessler G, Li E, Ma S, Yu D, Gebauer J, Baumann U, Liu X, Han Z, Chang J, Parker JE, Chai J Science. 2022 Jul 29;377(6605):eabq8180. doi: 10.1126/science.abq8180. Epub 2022 , Jul 29. PMID:35857644[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Arabidopsis | Large Structures | Chai JJ | Han ZF | Huang SJ | Jia AL
