Plant growth promoting bacteria improve growth and phytostabilization potential of Zea mays under chromium and drought stress by altering photosynthetic and antioxidant responses

Drought in heavy metal polluted arid and semiarid regions severely inhibits the plant growth and phytoremediation potential by affecting photosynthesis, antioxidant defense mechanism, and other biochemical processes. In the present study, we explored the role of plant growth-promoting bacteria (PGPB) on Zea mays growth and phytoremediation efficiency in Chromium (Cr) contaminated soils under drought stress by assessing plant stress tolerance, photosynthetic gas exchange activities, chlorophyll fluorescence, and Cr accumulation. Two efficient Cr and drought resistant PGPB with the potential to reduce Cr(VI) to Cr(III) and produce plant growth-promoting metabolites even under Cr, drought, or Cr+drought stress conditions were isolated and identified as Providencia sp. (TCR05) and Proteus mirabilis (TCR20). In pot experiments, the inoculation of TCR05 and TCR20 increased the plant growth, pigments, protein, phenolics, and relative water content and decreased the lipid peroxidation, proline, and superoxide dismutase activity under Cr, drought, or Cr+drought conditions. Irrespective of stress treatment, TCR05 and TCR20 also improved plant photosynthetic efficiency by increasing the CO2 assimilation rate, stomatal conductance to water vapor, transpiration rate, maximum quantum efficiency of PSII, actual quantum efficiency of PSII, electron transport rate, photochemical quenching, reducing the internal CO2 concentration and non-photochemical quenching. Besides, the PGPB decreased the translocation of Cr through immobilization of Cr in root. These results denoted that strains TCR05 and TCR20 could be a capable bio-inoculant for improving plant growth and phytostabilization practices in Cr contaminated sites even under water-limited conditions. © 2021 The AuthorsL.B.B thankful to the Science and Engineering Research Board (SERB), India for providing National Post-Doctoral Fellowship (Grant No. PDF/2017/001074 ). A.K., T, and M.R. are grateful for the “ Department of Science and Technology (DST), India (Project No. INT/RUS/RFBR/363 ) and Russian Foundation for Basic Research, Russia (Project No. 19-516-45006 ) bilateral research grant”. A.K. acknowledge the work support by Russian Science Foundation (Project No. 21-76-00011 ). Many thanks to Benedict Analin from the Department of Life Sciences, Central University of Tamil Nadu for helping to analyze photosynthetic parameters in the laboratory. The manuscript was written through the contributions of all authors

Comparison of ATP sulfurylase 2 from selenium hyperaccumulator Stanleya pinnata and non-accumulator Stanleya elata reveals differential intracellular localization and enzyme activity levels

Background: The plant Stanleya pinnata hyperaccumulates Se up to 0.5% of its dry weight in organic forms, whereas the closely related Stanleya elata does not hyperaccumulate Se. ATP sulfurylase (ATPS) can catalyze the formation of adenosine 5′-phosphoselenate (APSe) from ATP and selenate. We investigated the S. pinnata ATPS2 isoform (SpATPS2) to assess its possible role in Se hyperaccumulation. Methods: ATPS expression and activity was compared in the two Stanleya species. The ATPS2 protein sequences were modeled. Sub-cellular locations were analyzed using GFP fusions. Enzyme activity of purified recombinant SpATPS2 was measured. Results: ATPS2 transcript levels were six-fold higher in roots of S. pinnata relative to S. elata. Overall root ATPS enzyme activity was two-fold elevated in S. pinnata. Cloning and sequencing of SpATPS2 and S. elata ATPS2 (SeATPS2) showed the predicted SeATPS2 to be canonical, while SpATPS2, although very similar in its core structure, has unique features, including an interrupted plastid targeting signal due to a stop codon in the 5′ region of the coding sequence. Indeed GFP fusions revealed that SpATPS2 had exclusive cytosolic localization, while SeATPS2 showed dual localization in plastids and cytosol. SpATPS2 activity was inhibited by both sulfate and selenate, indicating that the enzyme acts on both substrates. Conclusions: The ATPS2 from S. pinnata differs from non-accumulator ATPS2 in its elevated expression and sub-cellular localization. It likely acts on both selente and sulfate substrates. General significance: These observations shed new light on the role of ATPS2 in the evolution of Se hyperaccumulation in plants. This article is part of a Special Issue entitled Selenium research in biochemistry and biophysics - 200 year anniversary issue, edited by Dr. Elias Arnér and Dr. Regina Brigelius-Flohe. © 2018 Elsevier B.V