scholarly journals Mutation of a Nucleotide-Binding Leucine-Rich Repeat Immune Receptor-Type Protein Disrupts Immunity to Bacterial Blight

2019 ◽  
Vol 181 (3) ◽  
pp. 1295-1313 ◽  
Author(s):  
Jiuyou Tang ◽  
Yiqin Wang ◽  
Wenchao Yin ◽  
Guojun Dong ◽  
Kai Sun ◽  
...  
Keyword(s):  
Bacterial Blight ◽  
Nucleotide Binding ◽  
Receptor Type ◽  
Leucine Rich Repeat ◽  
Immune Receptor ◽  
Type Protein

scholarly journals The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein

2015 ◽  
Vol 290 (41) ◽  
pp. 24945-24960 ◽  
Author(s):  
Stepan Fenyk ◽  
Philip D. Townsend ◽  
Christopher H. Dixon ◽  
Gerhard B. Spies ◽  
Alba de San Eustaquio Campillo ◽  
...  
Keyword(s):  
Nucleotide Binding ◽  
Leucine Rich Repeat ◽  
Immune Receptor

scholarly journals HSC70 regulates cold-induced caspase-1 hyperactivation by an autoinflammation-causing mutant of cytoplasmic immune receptor NLRC4

2019 ◽  
Vol 116 (43) ◽  
pp. 21694-21703 ◽  
Author(s):  
Akhouri Kishore Raghawan ◽  
Rajashree Ramaswamy ◽  
Vegesna Radha ◽  
Ghanshyam Swarup
Keyword(s):  
Nucleotide Binding ◽  
Negative Regulator ◽  
Interleukin 1Β ◽  
Temperature Sensitive ◽  
Leucine Rich Repeat ◽  
Immune Receptor ◽  
Caspase 1 ◽  
Heat Shock Cognate Protein ◽  
Lower Temperature ◽  
Cognate Protein

NLRC4 [nucleotide-binding domain and leucine-rich repeat (NLR) family, caspase recruitment domain (CARD) containing 4] is an innate immune receptor, which, upon detection of certain pathogens or internal distress signals, initiates caspase-1–mediated interleukin-1β maturation and an inflammatory response. A gain-of-function mutation, H443P in NLRC4, causes familial cold autoinflammatory syndrome (FCAS) characterized by cold-induced hyperactivation of caspase-1, enhanced interleukin-1β maturation, and inflammation. Although the H443P mutant shows constitutive activity, the mechanism involved in hyperactivation of caspase-1 by NLRC4-H443P upon exposure of cells to lower temperature is not known. Here, we show that heat shock cognate protein 70 (HSC70) complexes with NLRC4 and negatively regulates caspase-1 activation by NLRC4-H443P in human cells. Compared with NLRC4, the structurally altered NLRC4-H443P shows enhanced interaction with HSC70. Nucleotide binding- and leucine-rich repeat domains of NLRC4, but not its CARD, can engage in complex formation with HSC70. Knockdown of HSC70 enhances apoptosis-associated speck-like protein containing a CARD (ASC)-speck formation and caspase-1 activation by NLRC4-H443P. Exposure to subnormal temperature results in reduced interaction of NLRC4-H443P with HSC70, and an increase in its ability to form ASC specks and activate caspase-1. Unlike the NLRC4-H443P mutant, another constitutively active mutant (NLRC4-V341A) associated with autoinflammatory diseases, but not FCAS, showed neither enhanced interaction with HSC70 nor an increase in inflammasome formation upon exposure to subnormal temperature. Our results identify HSC70 as a negative regulator of caspase-1 activation by the temperature-sensitive NLRC4-H443P mutant. We also show that low-temperature–induced hyperactivation of caspase-1 by NLRC4-H443P is due to loss of inhibition by HSC70.

scholarly journals The Tomato Nucleotide-binding Leucine-rich Repeat Immune Receptor I-2 Couples DNA-binding to Nucleotide-binding Domain Nucleotide Exchange

2015 ◽  
Vol 291 (3) ◽  
pp. 1137-1147 ◽  
Author(s):  
Stepan Fenyk ◽  
Christopher H. Dixon ◽  
William H. Gittens ◽  
Philip D. Townsend ◽  
Gary J. Sharples ◽  
...  
Keyword(s):  
Dna Binding ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Exchange ◽  
Nucleotide Binding Domain ◽  
Immune Receptor

scholarly journals Nucleotide-Binding Leucine-Rich Repeat Genes CsRSF1 and CsRSF2 Are Positive Modulators in the Cucumis sativus Defense Response to Sphaerotheca fuliginea

2021 ◽  
Vol 22 (8) ◽  
pp. 3986
Author(s):  
Xue Wang ◽  
Qiumin Chen ◽  
Jingnan Huang ◽  
Xiangnan Meng ◽  
Na Cui ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Defense Response ◽  
Nucleotide Binding ◽  
Plant Defense Response ◽  
Sphaerotheca Fuliginea ◽  
Leucine Rich Repeat ◽  
Transcript Levels ◽  
Yield And Quality ◽  
Leucine Rich Repeats ◽  
Exogenous Substances

Cucumber powdery mildew caused by Sphaerotheca fuliginea is a leaf disease that seriously affects cucumber’s yield and quality. This study aimed to report two nucleotide-binding site-leucine-rich repeats (NBS-LRR) genes CsRSF1 and CsRSF2, which participated in regulating the resistance of cucumber to S. fuliginea. The subcellular localization showed that the CsRSF1 protein was localized in the nucleus, cytoplasm, and cell membrane, while the CsRSF2 protein was localized in the cell membrane and cytoplasm. In addition, the transcript levels of CsRSF1 and CsRSF2 were different between resistant and susceptible cultivars after treatment with exogenous substances, such as abscisic acid (ABA), methyl jasmonate (MeJA), salicylic acid (SA), ethephon (ETH), gibberellin (GA) and hydrogen peroxide (H2O2). The expression analysis showed that the transcript levels of CsRSF1 and CsRSF2 were correlated with plant defense response against S. fuliginea. Moreover, the silencing of CsRSF1 and CsRSF2 impaired host resistance to S. fuliginea, but CsRSF1 and CsRSF2 overexpression improved resistance to S. fuliginea in cucumber. These results showed that CsRSF1 and CsRSF2 genes positively contributed to the resistance of cucumber to S. fuliginea. At the same time, CsRSF1 and CsRSF2 genes could also regulate the expression of defense-related genes. The findings of this study might help enhance the resistance of cucumber to S. fuliginea.

Tracing the origin and evolutionary history of plant nucleotide-binding site-leucine-rich repeat (NBS-LRR) genes

2011 ◽  
Vol 193 (4) ◽  
pp. 1049-1063 ◽  
Author(s):  
Jia-Xing Yue ◽  
Blake C. Meyers ◽  
Jian-Qun Chen ◽  
Dacheng Tian ◽  
Sihai Yang
Keyword(s):  
Binding Site ◽  
Evolutionary History ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Leucine Rich Repeat ◽  
History Of
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