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Plants and plant products are key to the survival of life on earth. Despite this fact, the significance of plant biochemistry is often underrepresented in science curricula. We designed an innovative laboratory activity to engage students in learning about the biochemical properties of natural polymers produced by plants. The focus of the hands-on activity is on mucilages and gums, which contain complex polysaccharides that have applications in industry. The 1.5-h activity is organized into three laboratory exercises. It begins with a demonstration of the water absorption property of seed coat mucilage upon hydration of seeds from psyllium, a plant that is grown commercially for mucilage production. The second exercise involves microscopy of a variety of plant seeds stained with ruthenium red dye to visualize pectin polysaccharides of the seed mucilage. Students learn about phenotypic variation among plant species and how the seed coat mucilage is beneficial to keep seeds hydrated during germination. The third exercise highlights an industrial application of plant gums as adhesives. The students prepare edible glue made with gum arabic, a type of plant polymer from the dried exudate of the "Acacia" plant. This three-part activity has been implemented in conjunction with a Girls Researching Our World (GROW) summer workshop for sixth to eighth graders over a 4-year period. It may be adapted as a laboratory activity for students of all ages, for example, to enhance biochemistry education for high-school students or undergraduate non-majors.

Summary Plant homeodomain leucine zipper IV (HD‐Zip IV) transcription factors (TFs) contain an evolutionarily conserved steroidogenic acute regulatory protein (StAR)‐related lipid transfer (START) domain. While the START domain is required for TF activity, its presumed role as a lipid sensor is not clear. Here we used tandem affinity purification from Arabidopsis cell cultures to demonstrate that PROTODERMAL FACTOR2 (PDF2), a representative member that controls epidermal differentiation, recruits lysophosphatidylcholines (LysoPCs) in a START‐dependent manner. Microscale thermophoresis assays confirmed that a missense mutation in a predicted ligand contact site reduces lysophospholipid binding. We additionally found that PDF2 acts as a transcriptional regulator of phospholipid‐ and phosphate (Pi) starvation‐related genes and binds to a palindromic octamer with consensus to a Pi response element. Phospholipid homeostasis and elongation growth were altered in pdf2 mutants according to Pi availability. Cycloheximide chase experiments revealed a role for START in maintaining protein levels, and Pi starvation resulted in enhanced protein destabilization, suggesting a mechanism by which lipid binding controls TF activity. We propose that the START domain serves as a molecular sensor for membrane phospholipid status in the epidermis. Our data provide insights toward understanding how the lipid metabolome integrates Pi availability with gene expression. [ABSTRACT FROM AUTHOR]

Efforts to identify and introduce single genes that could maintain or increase cotton production in water-limited production settings have resulted in extremely limited success. The primary objective of this investigation was to test whether overexpression of the tomato fructokinase gene, LeFRK1, in field-grown cotton could improve fiber yield under variable growth conditions and contrasting irrigation levels in warm semi-arid environments characteristic of the Southern High Plains. A secondary goal was to determine whether a larger field-scale experiment might be justified based upon the results of this exploratory work. Cotton overexpressing LeFRK1 was field grown in small plots for three years under irrigation, contrasting irrigation levels, or without irrigation. Increased yield was found when comparing all LeFRK1 lines relative to that of the control line, though seasonal and plant-to-plant variability limited confidence in the extension of results to production scale. We hypothesized that yield improvements resulted from a suite of responses arising from increased availability of photosynthate at the leaf to the whole-plant level to developing fruits. The results suggested that LeFRK1 overexpression might be a viable approach to improving cotton yield in warm, semi-arid environments characteristic of the southwestern U.S. However, field trials under agronomically relevant systems and at agronomically relevant scales are needed to confirm these findings. [ABSTRACT FROM AUTHOR]

GLABRA2 (GL2), a class IV homeodomain leucine-zipper (HD-Zip IV) transcription factor (TF) from Arabidopsis, is a developmental regulator of specialized cell types in the epidermis. GL2 contains a monopartite nuclear localization sequence (NLS) that is conserved in most HD-Zip IV members across the plants. We demonstrate that NLS mutations affect nuclear transport and result in a loss-of-function phenotypes. NLS fusions to EYFP show that it is sufficient for nuclear localization in roots and trichomes. Despite partial overlap of the NLS with the homeodomain, genetic dissection indicates that nuclear localization and DNA binding are separable functions. Affinity purification of GL2 from plants followed by MS-based proteomics identified Importin α (IMPα) isoforms as potential GL2 interactors. NLS structural prediction and molecular docking studies with IMPα-3 revealed major interacting residues. Cytosolic yeast two-hybrid assays and co-immunoprecipitation experiments with recombinant proteins verified NLS-dependent interactions between GL2 and several IMPα isoforms. IMPα triple mutants (impα-1,2,3) exhibit abnormal trichome formation and defects in GL2 nuclear localization in trichomes, consistent tissue-specific and redundant functions of IMPα isoforms. Taken together, our findings provide mechanistic evidence for IMPα-dependent nuclear localization of GL2 in Arabidopsis, a process that is critical for cell-type differentiation of the epidermis., (© The Author(s) 2024. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.)