AtPPRT3, a novel E3 ubiquitin ligase, plays a positive role in ABA signaling
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ORIGINAL ARTICLE
AtPPRT3, a novel E3 ubiquitin ligase, plays a positive role in ABA signaling Yu Liu1 · Lu Peng1 · Xuemeng Gao1 · Yingying Liu1 · Zhibin Liu1 · Xufeng Li1 · Yi Yang1 · Jianmei Wang1 Received: 8 May 2020 / Accepted: 23 July 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Key message The RING-type E3 ligase AtPPRT3 participates in the plant ABA responding as a positive regulator. Abstract E3 ubiquitin ligase, alike of classic plant stress resistance proteins, plays a vital role in regulating the degradation of stress-related proteins. In this study, we investigated the function of the RING-type E3 ubiquitin ligase AtPPRT3 in the ABA signaling pathway. AtPPRT3, located in the endoplasmic reticulum membrane, is involved in ABA signaling. The transcriptional expression of AtPPRT3 was induced by ABA, and the promoter region upstream of AtPPRT3 contains the ABA-responsive element (ABRE). Additionally, the β-glucuronidase (GUS) gene driven by the AtPPRT3 promoter was upregulated in transgenic plants after ABA treated. We obtained AtPPRT3 function-deficient mutants atpprt3-1, atpprt3-2, and AtPPRT3 over-expressing lines (OE4 and OE5). In this study, atpprt3-1 and atpprt3-2 were less sensitive to exogenous ABA compared to Col-0, whereas OE4 and OE5 were more sensitive. Moreover, AtPPRT3 promotes ABA-mediated stomatal closure and inhibits water loss in Arabidopsis thaliana. After exogenous ABA treated, the transcriptional expression levels of AtDREB2A, AtKIN1, AtRD29A, AtERD10 and AtRD29B were up-regulated to greater extents in OEs and lower extents in atpprt3-1 and atpprt3-2 compared to Col-0. These results suggest that AtPPRT3 positively regulates ABA signaling in A. thaliana. Keywords AtPPRT3 · Arabidopsis thaliana · positive regulator · ABA signaling
Introduction The regulatory network in plants is composed of a variety of enzymatic cascade reactions. The protein synthesis pathway and the degradation pathway need to work together to Communicated by Günther Hahne. Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00299-020-02575-3) contains supplementary material, which is available to authorized users.
maintain the dynamic balance of protein levels in plants. The ubiquitin–proteasome system (UPS) is a vital protein degradation pathway in plants, where E3 ubiquitin ligase determines the specificity of the ubiquitination pathway (Xu and Xue 2019). UPS is divided into two processes. Primarily, E1 ubiquitin-activating enzyme, E2 ubiquitin-binding enzyme, and E3 ubiquitin ligase cooperate to complete polyubiquitination modification of the target protein (Pickart 2001). Subsequently, the target protein is modified by polyubiquitination while recognized, then degraded by the
* Jianmei Wang [email protected]; [email protected]
Zhibin Liu [email protected]
Yu Liu [email protected]
Xufeng Li [email protected]
Lu Peng [email protected]
Yi Yang [email protected]
Xuemeng Gao [email protected]
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