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Updated: Apr 21, 2026

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
Bacterial effector modulation of host E3 ligase activity suppresses PAMP-triggered immunity in rice
Kazuya Ishikawa1, Koji Yamaguchi1, Kazuaki Sakamoto1
1Department of Advanced Bioscience, Graduate School of Agriculture, Kinki University, 3327-204 Nakamachi, Nara 631-8505, Japan.
Abstract:
Pathogen effector proteins are delivered to host cells to suppress plant immunity. However, the mechanisms by which effector proteins function are largely unknown. Here we show that expression of XopP(Xoo), an effector of rice pathogen Xanthomonas oryzae pv. oryzae, in rice strongly suppresses peptidoglycan (PGN)- and chitin-triggered immunity and resistance to X. oryzae. XopP(Xoo) targets OsPUB44, a rice ubiquitin E3 ligase with a unique U-box domain. We find that XopP(Xoo) directly interacts with the OsPUB44 U-box domain and inhibits ligase activity. Two amino-acid residues specific for the OsPUB44 U-box domain are identified, which are responsible for the interaction with XopP(Xoo). Silencing of OsPUB44 suppresses PGN- and chitin-triggered immunity and X. oryzae resistance, indicating that OsPUB44 positively regulates immune responses. Thus, it is likely that XopP(Xoo) suppresses immune responses by directly interacting with and inhibiting a positive regulator of plant immunity.
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