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1.
Physiol Mol Biol Plants ; 29(7): 905-925, 2023 Jul.
Article in English | MEDLINE | ID: mdl-37649886

ABSTRACT

The basic leucine zipper (bZIP) protein transcription factors are known to modulate development, plant growth, metabolic response, and resistance to several biotic and abiotic stressors and have been widely studied in the model plant Arabidopsis thaliana. However, no comprehensive information about the bZIP transcription factor family in Artemisia annua has been explored to date. In this genome-wide study, we identified 61 bZIP TFs after removing false positives and incomplete sequences from Artemisia annua. Seven highly expressed homolog AabZIP TF genes under UV-B and differential light conditions in different tissues were identified from the publicly available microarray dataset as having their cis-regulatory elements involved in, flavonoids biosynthesis, seed-specific gene regulation, stress responses, and metabolic regulation. In-silico analysis and electrophoretic mobility shift assay (EMSA) confirmed the interaction of AabZIP19 TF over the AaPAL1 promoter in order to regulate the phenolics and flavonoid biosynthesis via the phenylpropanoid pathway. Further, RT-PCR analysis has been carried out to validate the transcript levels of selected AabZIP genes under white light, red light, blue light (45 min), and UV-B exposure (12 and 24 h). These genes have their highest expression levels under UV-B and blue light exposure, in contrast with white light. Therefore, the detection of ROS through staining confirms the accumulation of superoxide radicals and H2O2, and in addition to reducing ROS accumulation under UV-B and blue light irradiation, total phenols and flavonoids are significantly enhanced. This study laid the groundwork for deciphering the possible role of AabZIP TFs under different light stress-responsive conditions and in the regulation of secondary metabolism. Supplementary Information: The online version contains supplementary material available at 10.1007/s12298-023-01338-0.

3.
Int J Biol Macromol ; 185: 277-286, 2021 Aug 31.
Article in English | MEDLINE | ID: mdl-34147526

ABSTRACT

Members of group Bacillus are most widely occurring microbes in agricultural soil and they affect crop health in various ways. They directly stimulate plant growth either by augmenting nutrients availability, invigorating plants' defence mechanisms; repressing soil-borne phytopathogens or by producing growth-regulating hormones like auxins and cytokinins. It is a well known fact that indole-3- acetic acid (a type of auxin) is a vital biologically active phytohormone excreted by certain Bacillus species, but its molecular mechanism has not yet been described. In this study, the auxin efflux carrier gene is isolated from the metagenome of the Tapta Kund hot spring, Uttrakhand, India. In addition, auxin efflux carrier (AEC) transporter protein of Bacillus licheniformis is modeled and the 318 amino acid residues long protein was found homologous to the apical sodium-dependent bile acid transporter (ASBT) of Yersinia frederiksnii, with 10 transmembrane segments (TM1-10) split into different domains: a panel domain defined by TM1, 2, 6 and 7; and a core domain defined by TM3-5 and 8-10. Finally, the predicted Bacillus licheniformis AEC protein has also been phylogenetically evaluated and its detailed molecular transport mechanism was worked out using molecular dynamics simulation analysis. Conclusively, this study demonstrates the efflux mechanism of the substrate, Indole 3- acetic acid by AEC transporter protein.


Subject(s)
Bacillus licheniformis/isolation & purification , Hot Springs/microbiology , Indoleacetic Acids/metabolism , Membrane Transport Proteins/chemistry , Membrane Transport Proteins/genetics , Amino Acid Sequence , Bacillus licheniformis/genetics , Bacillus licheniformis/metabolism , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Biological Transport , India , Membrane Transport Proteins/metabolism , Metagenomics , Models, Molecular , Molecular Dynamics Simulation , Protein Domains , Protein Structure, Tertiary
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