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Wound-induced rgs-CaM gets ready for counterresponse to an early stage of viral infection

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/50867

Title: Wound-induced rgs-CaM gets ready for counterresponse to an early stage of viral infection
Authors: Tadamura, Kazuki Browse this author
Nakahara, Kenji S Browse this author →KAKEN DB
Masuta, Chikara Browse this author →KAKEN DB
Uyeda, Ichiro Browse this author →KAKEN DB
Keywords: PAMPs
RNAi
autophagy
calmodulin-like protein
pattern recognition receptor
plant innate immunity
Issue Date: Dec-2012
Publisher: Landes Bioscience
Journal Title: Plant Signaling & Behavior
Volume: 7
Issue: 12
Start Page: 1548
End Page: 1551
Publisher DOI: 10.4161/psb.22369
Abstract: Plants and animals can recognize the invasion of pathogens through their perception of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs). Plant PRRs identified have been exclusively receptor-like kinases/proteins (RLK/Ps), and no RLK/P that can detect viruses has been identified to date. RNA silencing (RNA interference, RNAi) is regarded as an antiviral basal immunity because the majority of plant viruses has RNA as their genomes and encode RNA silencing suppressor (RSS) proteins to counterattack antiviral RNAi. Many RSSs were reported to bind to double-stranded RNAs (dsRNAs), which are regarded as viral PAMPs. We have recently identified a tobacco calmodulin (CaM)-like protein, rgs-CaM, as a PRR that binds to diverse viral RSSs through its affinity for the dsRNA-binding domains. Because rgs-CaM seems to target RSSs for autophagic degradation with self-sacrifice, the expression level of rgs-CaM is important for antiviral activity. Here, we found that the rgs-CaM expression was induced immediately (within 1 h) after wounding at a wound site on tobacco leaves. Since the invasion of plant viruses is usually associated with wounding, and several hours are required for viruses to replicate to a detectable level in invaded cells, the wound-induced expression of rgs-CaM seems to be linked to its antiviral function, which should be ready before the virus establishes infection. CaMs and CaM-like proteins usually transduce calcium signals through their binding to endogenous targets. Therefore, rgs-CaM is a unique CaM-like protein in terms of binding to exogenous targets and functioning as an antiviral PRR.
Type: article (author version)
URI: http://hdl.handle.net/2115/50867
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 中原 健二

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