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Deciphering the Role of Arabidopsis TIR-NBS 2 Receptor in Cell Death Signaling in Nicotiana benthamiana
Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
- 1 Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
- 2 Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
- 3 Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
- 4 Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
- 5 Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
- 6 Fuzhou Medical University (Formerly Known as Fuzhou Medical College of Nanchang University), Fuzhou, China
Advances in Bioscience and Biotechnology·Volume 16 (2025)·Pages 437–445·Published 16 October 2025·DOI10.4236/abb.2025.1610028
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Abstract
The truncated Toll/interleukin-1 receptor-NBS (TIR-NBS) proteins act significant role in immunity. Previous articles reported an Arabidopsis thaliana resistance protein TIR-NBS 2 (TN2) can arise violent cell death in tobacco ( Nicotiana benthamiana ) leaves. Nevertheless, the specific mechanism by which this protein strikes cell death is generally poor. Here, we preliminarily dissected the activation mechanism of TN2 immune receptor in N. benthamiana . The outcomes of the transient analysis attested that the TN2-TIR domain itself is enough to cell-death induction. The yellow fluorescent protein (YFP)-tagged TN2 and TN2-TIR were major localized to the cytoplasm, which was considered essential to the function of the TN2 and TN2-TIR. Additionally, the cell-death-inducing activity of TN2 can be inhibited by the full-length EXO70B1 instead of its truncated fragments. These research findings provided some clues for understanding the activation mechanism of TN2.
KeywordsCell DeathTIR-NBS 2EXO70B1Nicotiana benthamiana
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