AtPPRT3, a novel E3 ubiquitin ligase, plays a positive role in ABA signaling.

Abstract

The RING-type E3 ligase AtPPRT3 participates in the plant ABA responding as a positive regulator. 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 up-regulated 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.