5年連続の選出（Cross-Field – 2018, 2022; Plant and Animal Science – 2019, 2020, 2021）
寺内良平教授がClarivate社 Highly Cited Researchers 2022 （2022年度 高被引用論文著者）に選出されました
5年連続の選出（Cross-Field – 2018, 2022; Plant and Animal Science – 2019, 2020, 2021）
5年連続の選出（Cross-Field – 2018, 2022; Plant and Animal Science – 2019, 2020, 2021）
堺俊之（助教）が日本育種学会優秀発表賞を受賞 / 第142回講演会（2022年度秋季大会、9月開催）
工藤葵（修士二回生）がポスター賞とAI賞を受賞 / 挑戦的両性花原理 若手の会（2022年10月開催）
工藤葵（修士二回生）が挑戦的両性花原理 若手の会（2022年10月開催）でポスター賞とAI賞を受賞しました。
挑戦的両性花原理 : https://www.ige.tohoku.ac.jp/prg/flower/
Publications リストを更新しました
次の論文をPublicationリストに追加しました。
Chia, K.-S., Kourelis, J., Vickers, M., Sakai, T., Kamoun, S., & Carella, P. (2022). The N-terminal executioner domains of NLR immune receptors are functionally conserved across major plant lineages. BioRxiv, 2022.10.19.512840. https://doi.org/10.1101/2022.10.19.512840 de la Concepcion, J. C., Fujisaki, K., Bentham, A. R., Cruz Mireles, N., Sanchez de Medina Hernandez, V., Shimizu, M., Lawson, D. M., Kamoun, S., Terauchi, R. & Banfield, M. J. (2022). A blast fungus zinc-finger fold effector binds to a hydrophobic pocket in host Exo70 proteins to modulate immune recognition in rice. Proceedings of the National Academy of Sciences, 119(43), e2210559119. https://doi.org/10.1073/pnas.2210559119
Rice apoplastic CBM1-interacting protein counters blast pathogen invasion by binding conserved carbohydrate binding module 1 motif of fungal proteins
This paper has been published in which Prof. Terauchi is the corresponding author.
Takeda, T., Takahashi, M., Shimizu, M., Sugihara, Y., Yamashita, T., Saitoh, H., Fujisaki, K., Ishikawa, K., Utsushi, H., Kanzaki, E., Sakamoto, Y., Abe, A., & Terauchi, R. (2022). Rice apoplastic CBM1-interacting protein counters blast pathogen invasion by binding conserved carbohydrate binding module 1 motif of fungal proteins. PLOS Pathogens, 18(9), e1010792-. https://doi.org/10.1371/journal.ppat.1010792
Abstract
When infecting plants, fungal pathogens secrete cell wall-degrading enzymes (CWDEs) that break down cellulose and hemicellulose, the primary components of plant cell walls. Some fungal CWDEs contain a unique domain, named the carbohydrate binding module (CBM), that facilitates their access to polysaccharides. However, little is known about how plants counteract pathogen degradation of their cell walls. Here, we show that the rice cysteine-rich repeat secretion protein OsRMC binds to and inhibits xylanase MoCel10A of the blast fungus pathogen Magnaporthe oryzae, interfering with its access to the rice cell wall and degradation of rice xylan. We found binding of OsRMC to various CBM1-containing enzymes, suggesting that it has a general role in inhibiting the action of CBM1. OsRMC is localized to the apoplast, and its expression is strongly induced in leaves infected with M. oryzae. Remarkably, knockdown and overexpression of OsRMC reduced and enhanced rice defense against M. oryzae, respectively, demonstrating that inhibition of CBM1-containing fungal enzymes by OsRMC is crucial for rice defense. We also identified additional CBM-interacting proteins (CBMIPs) from Arabidopsis thaliana and Setaria italica, indicating that a wide range of plants counteract pathogens through this mechanism.
Author summary
Plants have evolved various activity-inhibiting proteins as a defense against fungal cell wall-degrading enzymes (CWDEs), but how plants counteract the function of fungal enzymes containing carbohydrate binding modules (CBMs) remains unknown. Here, we demonstrate that OsRMC, a member of the cysteine-rich repeat secretion protein family, interacts with fungal CBM1. OsRMC binding to CBM1 of a blast fungal xylanase blocks access to cellulose, resulting in the inhibition of xylanase enzymatic activity. Our study provides significant insights into plant countermeasures against CWDEs in the apoplastic space during plant-fungal pathogen interactions. It also reveals a molecular function of the DUF26 domain widely distributed in plant proteins.
