Publications of NIPGR Scientists

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Subject: search.filters.subject.E3 ligase

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    Rice A20/AN1 protein, OsSAP10, confers water-deficit stress tolerance via proteasome pathway and positive regulation of ABA signaling in Arabidopsis
    (Springer Nature Publishing AG, 2024) Vashisth, Vishal; Sharma, Gunjan; Giri, Jitender; Sharma, Arun K.; Tyagi, Akhilesh K.
    Overexpression of rice A20/AN1 zinc-finger protein, OsSAP10, improves water-deficit stress tolerance in Arabidopsis via interaction with multiple proteins. Stress-associated proteins (SAPs) constitute a class of A20/AN1 zinc-finger domain containing proteins and their genes are induced in response to multiple abiotic stresses. The role of certain SAP genes in conferring abiotic stress tolerance is well established, but their mechanism of action is poorly understood. To improve our understanding of SAP gene functions, OsSAP10, a stress-inducible rice gene, was chosen for the functional and molecular characterization. To elucidate its role in water-deficit stress (WDS) response, we aimed to functionally characterize its roles in transgenic Arabidopsis, overexpressing OsSAP10. OsSAP10 transgenics showed improved tolerance to water-deficit stress at seed germination, seedling and mature plant stages. At physiological and biochemical levels, OsSAP10 transgenics exhibited a higher survival rate, increased relative water content, high osmolyte accumulation (proline and soluble sugar), reduced water loss, low ROS production, low MDA content and protected yield loss under WDS relative to wild type (WT). Moreover, transgenics were hypersensitive to ABA treatment with enhanced ABA signaling and stress-responsive genes expression. The protein-protein interaction studies revealed that OsSAP10 interacts with proteins involved in proteasomal pathway, such as OsRAD23, polyubiquitin and with negative and positive regulators of stress signaling, i.e., OsMBP1.2, OsDRIP2, OsSCP and OsAMTR1. The A20 domain was found to be crucial for most interactions but insufficient for all interactions tested. Overall, our investigations suggest that OsSAP10 is an important candidate for improving water-deficit stress tolerance in plants, and positively regulates ABA and WDS signaling via protein-protein interactions and modulation of endogenous genes expression in ABA-dependent manner.
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    Ubiquitination from the perspective of plant pathogens
    (Oxford University Press, 2023) Sharma, Shambhavi; Prasad, Ashish; Prasad, Manoj
    The constant battle of survival between pathogens and host plants has played a crucial role in shaping the course of their co-evolution. However, the major determinants of the outcome of this ongoing arms race are the effectors secreted by pathogens into the host cells. These effectors perturb the defense responses of plants to promote their successful infection. In recent years, the extensive research in the area of effector biology has reported an increase in the repertoire of pathogenic effectors that mimics or targets the conserved ubiquitin proteasomal pathway. The role of ubiquitin mediated degradation pathway has been well known to be indispensable for various aspects of plant’s life, thus targeting or mimicking it seems to be a smart strategy adopted by pathogens in their favor. Therefore, this review summarizes the recent findings on how some pathogenic effectors mimics or act as one of the components of ubiquitin proteasomal machinery while others directly target the plant’s ubiquitin proteasomal system.
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    Ubiquitination: a tool for plant adaptation to changing environments
    (Springer Nature, 2018) Mandal, Arunava; Sharma, Namisha; Muthamilarasan, Mehanathan; Prasad, Manoj
    Post-translational modifcations namely ubiquitination, phosphorylation, methylation and acetylation play distinct roles in regulating the growth and development of plants. Among these, the ubiquitination regulates the abundance, activities, subcellular compartmentalization and trafcking of regulatory proteins involved in diverse developmental as well as stress-responsive processes. The ubiquitin–proteasome system (UPS) involves fve essential components namely ubiquitin, ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3) and the intact 26S proteasome. The E3 ubiquitin ligase is the major component of UPS that recognizes and tethers poly-ubiquitins on the target proteins. Owing to its specifcity of substrate recognition, the E3 ubiquitin ligase contributes not only to the proteome plasticity of the cell but also regulates the plant’s response to environmental cues. In this context, the review summarizes the components involved in UPS and elaborates the role of E3 ubiquitin ligase in biotic and abiotic stress responses.