Abstract

E3 ubiquitin ligases are involved in many processes, regulating the response to biotic and abiotic stresses. In this study, 11 E3 ubiquitin ligase genes from Arabidopsis, which were hypothesized to function in response to biotic or abiotic stresses were selected, and the homologous genes in rice were found. Their functions were analyzed in rice. These 11 E3 ubiquitin ligase genes showed different patterns of expression under different treatments. The BMV:OsPUB39-infiltrated seedlings showed decreased resistance to Magnaporthe grisea (M. grisea) when compared with BMV:00-infiltrated seedlings, whereas the BMV:OsPUB34- and BMV:OsPUB33-infiltrated seedlings showed increased resistance. The involvement of these genes in the resistance against M. grisea may be attributed to the regulation of the accumulation of reactive oxygen species (ROS) and expression levels of defense-related genes. Seedlings infiltrated by BMV:OsATL69 showed decreased tolerance to drought stress, whereas BMV:OsPUB33-infiltraed seedlings showed increased tolerance, possibly through the regulation of proline content, sugar content, and expression of drought-responsive genes. BMV:OsATL32-infiltrated seedlings showed decreased tolerance to cold stress by regulating malondialdehyde (MDA) content and the expression of cold-responsive genes.

Highlights

  • Ubiquitination is a post-translational modification, involved in many processes

  • The expression of OsPUB39, OsPUB34, and OsPUB33 was strongly induced by the inoculation of M. grisea in incompatible interaction, whereas the expression of other genes showed no significant difference between the treatment and control at the time point we test (Figure 1A)

  • The expression levels of OsPUB39, OsPUB34, and OsPUB33 were strongly induced by the hormones SA, jasmonic acid (JA), and ACC, whereas the expression levels of other genes were unaffected (Figure 1B)

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Summary

Introduction

Ubiquitination is a post-translational modification, involved in many processes. Ubiquitination is mediated by three sequential ubiquitin enzymes, E1 (the ubiquitin-activating enzyme), E2 (the ubiquitin-conjugating enzyme), and E3 (the ubiquitin ligase). E3 ubiquitin ligases have been reported to function in several processes, including the responses to biotic and abiotic stresses (Ariani et al, 2017; Sun et al, 2019, 2022; Zhang et al, 2019; Du et al, 2021; Sharma et al, 2021). E3 ubiquitin ligases are involved in response to biotic stresses. The ATL subfamily that contains the conserved RING-H2 domain is activated by the elicitor and plays important roles in disease resistance, possibly through the regulation of the elicitor-signaling pathway, including chitin (Serrano and Guzman, 2004; Berrocal-Lobo et al, 2010; Ni et al, 2010; Chen et al, 2017; Deng et al, 2017). The U-box domain family of E3 ubiquitin ligases plays important roles in defense response.

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