scholarly journals A Truncated TIR-NBS Protein TN10 Pairs with Two Clustered TIR-NBS-LRR Immune Receptors and Contributes to Plant Immunity in Arabidopsis

2021 ◽  
Vol 22 (8) ◽  
pp. 4004
Author(s):  
Yongming Chen ◽  
Guitao Zhong ◽  
Huiren Cai ◽  
Renjie Chen ◽  
Na Liu ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Plant Disease Resistance ◽  
Plant Immunity ◽  
Interleukin 1 ◽  
Chromosome 1 ◽  
Immune Receptors ◽  
Arabidopsis Ecotype ◽  
Genomic Arrangement ◽  
Tir Domains ◽  
Encoding Genes

The encoding genes of plant intracellular nucleotide-binding site (NBS) and leucine-rich repeat (LRR) domain receptors (NLRs) often exist in the form of a gene cluster. Several recent studies demonstrated that the truncated Toll/interleukin-1 receptor-NBS (TIR-NBS) proteins play important roles in immunity. In this study, we identified a large TN gene cluster on Arabidopsis ecotype Col-0 chromosome 1, which included nine TN genes, TN4 to TN12. Interestingly, this cluster also contained two typical TIR-NBS-LRR genes: At1g72840 and At1g72860 (hereinafter referred to as TNL40 and TNL60, respectively), which formed head-to-head genomic arrangement with TN4 to TN12. However, the functions of these TN and TNL genes in this cluster are still unknown. Here, we showed that the TIR domains of both TNL40 and TNL60 associated with TN10 specifically. Furthermore, both TNL40TIR and TNL60TIR induced cell death in Nicotiana tabacum leaves. Subcellular localization showed that TNL40 mainly localized in the cytoplasm, whereas TNL60 and TN10 localized in both the cytoplasm and nucleus. Additionally, the expression of TNL40, TNL60, and TN10 were co-regulated after inoculated with bacterial pathogens. Taken together, our study indicates that the truncated TIR-NBS protein TN10 associates with two clustered TNL immune receptors, and may work together in plant disease resistance

scholarly journals Identification of Immune Related LRR-Containing Genes in Maize (Zea maysL.) by Genome-Wide Sequence Analysis

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Wei Song ◽  
Baoqiang Wang ◽  
Xinghua Li ◽  
Jianfen Wei ◽  
Ling Chen ◽  
...  
Keyword(s):  
Zea Mays ◽  
Plant Disease Resistance ◽  
Interleukin 1 ◽  
Protein Structures ◽  
Gene Clusters ◽  
Amino Acid Sequences ◽  
Leucine Rich Repeat ◽  
Immune Receptors ◽  
Genome Wide ◽  
First Time

A large number of immune receptors consist of nucleotide binding site-leucine rich repeat (NBS-LRR) proteins and leucine rich repeat-receptor-like kinases (LRR-RLK) that play a crucial role in plant disease resistance. Although many NBS-LRR genes have been previously identified inZea mays, there are no reports on identifying NBS-LRR genes encoded in the N-terminal Toll/interleukin-1 receptor (TIR) motif and identifying genome-wide LRR-RLK genes. In the present study, 151 NBS-LRR genes and 226 LRR-RLK genes were identified after performing bioinformatics analysis of the entire maize genome. Of these identified genes, 64 NBS-LRR genes and four TIR-NBS-LRR genes were identified for the first time. The NBS-LRR genes are unevenly distributed on each chromosome with gene clusters located at the distal end of each chromosome, while LRR-RLK genes have a random chromosomal distribution with more paired genes. Additionally, six LRR-RLK/RLPs including FLS2, PSY1R, PSKR1, BIR1, SERK3, and Cf5 were characterized inZea maysfor the first time. Their predicted amino acid sequences have similar protein structures with their respective homologues in other plants, indicating that these maize LRR-RLK/RLPs have the same functions as their homologues act as immune receptors. The identified gene sequences would assist in the study of their functions in maize.

scholarly journals TIR domains of plant immune receptors are NAD+-cleaving enzymes that promote cell death

Science ◽  
2019 ◽  
Vol 365 (6455) ◽  
pp. 799-803 ◽  
Author(s):  
Li Wan ◽  
Kow Essuman ◽  
Ryan G. Anderson ◽  
Yo Sasaki ◽  
Freddy Monteiro ◽  
...  
Keyword(s):  
Cell Death ◽  
Enzymatic Activity ◽  
Interleukin 1 ◽  
Adenosine Diphosphate ◽  
Immune Receptors ◽  
Cell Death Response ◽  
A Cell ◽  
Self Association ◽  
Activate Cell ◽  
Tir Domains

Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors activate cell death and confer disease resistance by unknown mechanisms. We demonstrate that plant Toll/interleukin-1 receptor (TIR) domains of NLRs are enzymes capable of degrading nicotinamide adenine dinucleotide in its oxidized form (NAD+). Both cell death induction and NAD+ cleavage activity of plant TIR domains require known self-association interfaces and a putative catalytic glutamic acid that is conserved in both bacterial TIR NAD+-cleaving enzymes (NADases) and the mammalian SARM1 (sterile alpha and TIR motif containing 1) NADase. We identify a variant of cyclic adenosine diphosphate ribose as a biomarker of TIR enzymatic activity. TIR enzymatic activity is induced by pathogen recognition and functions upstream of the genes enhanced disease susceptibility 1 (EDS1) and N requirement gene 1 (NRG1), which encode regulators required for TIR immune function. Thus, plant TIR-NLR receptors require NADase function to transduce recognition of pathogens into a cell death response.

scholarly journals TIR domains of plant immune receptors are 2',3'-cAMP/cGMP synthetases mediating cell death

2021 ◽  
Author(s):  
Dongli Yu ◽  
Wen Song ◽  
Eddie Yong Jun Tan ◽  
Li Liu ◽  
Yu Cao ◽  
...  
Keyword(s):  
Cell Death ◽  
Immune Responses ◽  
Interleukin 1 ◽  
Structural Data ◽  
Negative Regulator ◽  
Synthetase Activity ◽  
Leucine Rich Repeat ◽  
Tir Domain ◽  
Immune Receptors ◽  
Tir Domains

2′,3′-cAMP is a positional isomer of the well-established second messenger 3′,5′-cAMP, but little is known on the biology of this noncanonical cyclic nucleotide monophosphate (cNMP). Toll/interleukin-1 receptor (TIR) domains of nucleotide-binding leucine-rich repeat (NLR) immune receptors have NADase function necessary but insufficient to activate plant immune responses. Here we show that plant TIR proteins, besides being NADases, act as 2′,3′-cAMP/cGMP synthetases by hydrolyzing RNA/DNA. Structural data shows that a TIR domain adopts distinct oligomers with dual and exclusive enzymatic activity. Mutations specifically disrupting the synthetase activity abrogate TIR-mediated cell death in Nicotiana benthamiana, supporting an important role for these cNMPs in TIR signaling. Furthermore, the Arabidopsis negative regulator of TIR-NLR signaling, NUDT7 displays 2′,3′-cAMP/cGMP but not 3′,5′-cAMP/cGMP phosphodiesterase activity and suppresses cell death activity of TIRs in N. benthamiana. Our study identifies a novel family of 2′,3′-cAMP/cGMP synthetase and establishes a role for the noncanonical cNMPs in plant immune responses.

Interleukin-1 Gene Cluster Polymorphisms Are Associated with Nutritional Status and Inflammation in Patients with End-Stage Renal Disease

2005 ◽  
Vol 23 (5) ◽  
pp. 384-393 ◽  
Author(s):  
Yukio Maruyama ◽  
Louise Nordfors ◽  
Peter Stenvinkel ◽  
Olof Heimbürger ◽  
Peter Bárány ◽  
...  
Keyword(s):  
Nutritional Status ◽  
Renal Disease ◽  
Gene Cluster ◽  
End Stage Renal Disease ◽  
Interleukin 1 ◽  
Stage Renal Disease ◽  
End Stage

scholarly journals Toll9 from Bombyx mori functions as a pattern recognition receptor that shares features with Toll-like receptor 4 from mammals

2021 ◽  
Vol 118 (19) ◽  
pp. e2103021118
Author(s):  
Ruonan Zhang ◽  
Xiaofeng Li ◽  
Jie Zhang ◽  
Yanjun Li ◽  
Yuan Wang ◽  
...  
Keyword(s):  
Pattern Recognition ◽  
Bombyx Mori ◽  
Interleukin 1 ◽  
Structural Data ◽  
Pattern Recognition Receptor ◽  
Inflammatory Factors ◽  
Microbial Infection ◽  
Mammalian Tlrs ◽  
Tir Domains ◽  
Recognition Receptor

Toll/Toll-like receptors (TLRs) are key regulators of the innate immune system in both invertebrates and vertebrates. However, while mammalian TLRs directly recognize pathogen-associated molecular patterns, the insect Toll pathway is thought to be primarily activated by binding Spätzle cytokines that are processed from inactive precursors in response to microbial infection. Phylogenetic and structural data generated in this study supported earlier results showing that Toll9 members differ from other insect Tolls by clustering with the mammalian TLR4 group, which recognizes lipopolysaccharide (LPS) through interaction with myeloid differentiation-2 (MD-2)–like proteins. Functional experiments showed that BmToll9 from the silkmoth Bombyx mori also recognized LPS through interaction with two MD-2–like proteins, previously named BmEsr16 and BmPP, that we refer to in this study as BmMD-2A and BmMD-2B, respectively. A chimeric BmToll9–TLR4 receptor consisting of the BmToll9 ectodomain and mouse TLR4 transmembrane and Toll/interleukin-1 (TIR) domains also activated LPS-induced release of inflammatory factors in murine cells but only in the presence of BmMD-2A or BmMD-2B. Overall, our results indicate that BmToll9 is a pattern recognition receptor for LPS that shares conserved features with the mammalian TLR4–MD-2–LPS pathway.

scholarly journals Opposing functions of the plant TOPLESS gene family during SNC1-mediated autoimmunity

2020 ◽  
Author(s):  
Christopher M. Garner ◽  
Benjamin J. Spears ◽  
Jianbin Su ◽  
Leland Cseke ◽  
Samantha N. Smith ◽  
...  
Keyword(s):  
Immune System ◽  
Genetic Interaction ◽  
Plant Immunity ◽  
Family Members ◽  
Negative Regulator ◽  
Careful Study ◽  
Negative Effects ◽  
Activating Mutations ◽  
Immune Receptors ◽  
Regulatory Processes

AbstractRegulation of the plant immune system is important for controlling the specificity and amplitude of responses to pathogens and in preventing growth-inhibiting autoimmunity that leads to reductions in plant fitness. In previous work, we reported that SRFR1, a negative regulator of effector-triggered immunity, interacts with SNC1 and EDS1. When SRFR1 is non-functional in the Arabidopsis accession Col-0, SNC1 levels increase, causing a cascade of events that lead to autoimmunity phenotypes. Previous work showed that some members of the transcriptional co-repressor family TOPLESS interact with SNC1 to repress negative regulators of immunity. Therefore, to explore potential connections between SRFR1 and TOPLESS family members, we took a genetic approach that examined the effect of each TOPLESS member in the srfr1 mutant background. The data indicated that an additive genetic interaction exists between SRFR1 and two members of the TOPLESS family, TPR2 and TPR3, as demonstrated by increased stunting and elevated PR2 expression in srfr1 tpr2 and srfr1 tpr2 tpr3 mutants. Furthermore, the tpr2 mutation intensifies autoimmunity in the auto-active snc1-1 mutant, indicating a novel role of these TOPLESS family members in negatively regulating SNC1-dependent phenotypes. This negative regulation can also be reversed by overexpressing TPR2 in the srfr1 tpr2 background. Thus, this work uncovers diverse functions of individual members of the TOPLESS family in Arabidopsis and provides evidence for the additive effect of transcriptional and post-transcriptional regulation of SNC1.Author SummaryThe immune system is a double-edged sword that affords organisms with protection against infectious diseases but can also lead to negative effects if not properly controlled. Plants only possess an innate antimicrobial immune system that relies on rapid upregulation of defenses once immune receptors detect the presence of microbes. Plant immune receptors known as resistance proteins play a key role in rapidly triggering defenses if pathogens breach other defenses. A common model of unregulated immunity in the reference Arabidopsis variety Columbia-0 involves a resistance gene called SNC1. When the SNC1 protein accumulates to unnaturally high levels or possesses auto-activating mutations, the visible manifestations of immune overactivity include stunted growth and low biomass and seedset. Consequently, expression of this gene and accumulation of the encoded protein are tightly regulated on multiple levels. Despite careful study the mechanisms of SNC1 gene regulation are not fully understood. Here we present data on members of the well-known TOPLESS family of transcriptional repressors. While previously characterized members were shown to function in indirect activation of defenses, TPR2 and TPR3 are shown here to function in preventing high defense activity. This study therefore contributes to the understanding of complex regulatory processes in plant immunity.

scholarly journals Polymorphisms in the interleukin-1 (IL1) gene cluster are not associated with aggressive periodontitis in a large Caucasian population

Genomics ◽  
2008 ◽  
Vol 92 (5) ◽  
pp. 309-315 ◽  
Author(s):  
Andreas Fiebig ◽  
Søren Jepsen ◽  
Bruno G. Loos ◽  
Claudia Scholz ◽  
Christine Schäfer ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Interleukin 1 ◽  
Aggressive Periodontitis ◽  
Caucasian Population

scholarly journals d-Sedoheptulose-7-phosphate is a common precursor for the heptoses of septacidin and hygromycin B

2018 ◽  
Vol 115 (11) ◽  
pp. 2818-2823 ◽  
Author(s):  
Wei Tang ◽  
Zhengyan Guo ◽  
Zhenju Cao ◽  
Min Wang ◽  
Pengwei Li ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Carbon Chain ◽  
Side Chain ◽  
Hygromycin B ◽  
Nucleoside Antibiotics ◽  
Common Precursor ◽  
Encoding Genes ◽  
Poultry Farming

Seven-carbon-chain–containing sugars exist in several groups of important bacterial natural products. Septacidin represents a group of l-heptopyranoses containing nucleoside antibiotics with antitumor, antifungal, and pain-relief activities. Hygromycin B, an aminoglycoside anthelmintic agent used in swine and poultry farming, represents a group of d-heptopyranoses–containing antibiotics. To date, very little is known about the biosynthesis of these compounds. Here we sequenced the genome of the septacidin producer and identified the septacidin gene cluster by heterologous expression. After determining the boundaries of the septacidin gene cluster, we studied septacidin biosynthesis by in vivo and in vitro experiments and discovered that SepB, SepL, and SepC can convert d-sedoheptulose-7-phosphate (S-7-P) to ADP-l-glycero-β-d-manno-heptose, exemplifying the involvement of ADP-sugar in microbial natural product biosynthesis. Interestingly, septacidin, a secondary metabolite from a gram-positive bacterium, shares the same ADP-heptose biosynthesis pathway with the gram-negative bacterium LPS. In addition, two acyltransferase-encoding genes sepD and sepH, were proposed to be involved in septacidin side-chain formation according to the intermediates accumulated in their mutants. In hygromycin B biosynthesis, an isomerase HygP can recognize S-7-P and convert it to ADP-d-glycero-β-d-altro-heptose together with GmhA and HldE, two enzymes from the Escherichia coli LPS heptose biosynthetic pathway, suggesting that the d-heptopyranose moiety of hygromycin B is also derived from S-7-P. Unlike the other S-7-P isomerases, HygP catalyzes consecutive isomerizations and controls the stereochemistry of both C2 and C3 positions.

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