Root plasticity under abiotic stress

Abiotic stresses increasingly threaten existing ecological and agricultural systems across the globe. Plant roots perceive these stresses in the soil and adapt their architecture accordingly. This review provides insights into recent discoveries showing the importance of root system architecture (RSA) and plasticity for the survival and development of plants under heat, cold, drought, salt, and flooding stress. In addition, we review the molecular regulation and hormonal pathways involved in controlling RSA plasticity, main root growth, branching and lateral root growth, root hair development, and formation of adventitious roots. Several stresses affect root anatomy by causing aerenchyma formation, lignin and suberin deposition, and Casparian strip modulation. Roots can also actively grow toward favorable soil conditions and avoid environments detrimental to their development. Recent advances in understanding the cellular mechanisms behind these different root tropisms are discussed. Understanding root plasticity will be instrumental for the development of crops that are resilient in the face of abiotic stress

Solubilization, Activation, and Insecticidal Activity of Bacillus thuringiensis Serovar thompsoni HD542 Crystal Proteins▿

Cry15Aa protein, produced by Bacillus thuringiensis serovar thompsoni HD542 in a crystal together with a 40-kDa accompanying protein, is one of a small group of nontypical, less well-studied members of the Cry family of insecticidal proteins and may provide an alternative for the more commonly used Cry proteins in insect pest management. In this paper, we describe the characterization of the Cry15Aa and 40-kDa protein's biochemical and insecticidal properties and the mode of action. Both proteins were solubilized above pH 10 in vitro. Incubation of solubilized crystal proteins with trypsin or insect midgut extracts rapidly processed the 40-kDa protein to fragments too small to be detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas the Cry15 protein yielded a stable product of approximately 30 kDa. Protein N-terminal sequencing showed that Cry15 processing occurs exclusively at the C-terminal end. Cry15 protein showed in vitro hemolytic activity, which was greatly enhanced by preincubation with trypsin or insect gut extract. Larvae of the lepidopteran insects Manduca sexta, Cydia pomonella, and Pieris rapae were susceptible to crystals, and presolubilization of the crystals enhanced activity to P. rapae. Activity for all three species was enhanced by preincubation with trypsin. Larvae of Helicoverpa armigera and Spodoptera exigua were relatively insensitive to crystals, and activity against these insects was not enhanced by prior solubilization or trypsin treatment. The 40-kDa crystal protein showed no activity in the insects tested, nor did its addition or coexpression in Escherichia coli increase the activity of Cry15 in insecticidal and hemolytic assays

The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 Protein Complex Includes BRASSINOSTEROID-INSENSITIVE1

Arabidopsis thaliana SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 (SERK1) is a leucine-rich repeat receptor-like kinase (LRR-RLK) involved in the acquisition of embryogenic competence and in male sporogenesis. To determine the composition of the SERK1 signaling complex in vivo, we generated plants expressing the SERK1 protein fused to cyan fluorescent protein under SERK1 promoter control. The membrane receptor complex was immunoprecipitated from seedlings, and the coimmunoprecipitating proteins were identified using liquid chromatography/matrix-assisted laser desorption ionization–time of flight/mass spectrometry of the trypsin-released peptides. This approach identified two other LRR-RLKs, the BRASSINOSTEROID-INSENSITIVE1 (BRI1) receptor and its coreceptor, the SERK3 or BRI1-ASSOCIATED KINASE1 protein. In addition, KINASE-ASSOCIATED PROTEIN PHOSPHATASE, CDC48A, and 14-3-3ν were found. Finally, the MADS box transcription factor AGAMOUS-LIKE15 and an uncharacterized zinc finger protein, a member of the CONSTANS family, were identified as part of the SERK1 complex. Using blue native gel electrophoresis, we show that SERK1 and SERK3 are part of BRI1-containing multiple protein complexes with relative masses between 300 and 500 kD. The SERK1 mutant allele serk1-1 enhances the phenotype of the weak BRI1 allele bri1-119. Collectively, these results suggest that apart from SERK3, SERK1 is also involved in the brassinolide signaling pathway

Bacillus thuringiensis -endotoxin Cry1Ac domain III enhances activity against Heliothis virescens in some, but not all Cry1-Cry1Ac hybrids

Abstract We investigated the role of domain III of Bacillus thuringiensis -endotoxin Cry1Ac in determining toxicity against Heliothis virescens. Hybrid toxins, containing domain III of Cry1Ac with domains I and II of Cry1Ba, Cry1Ca, Cry1Da, Cry1Ea, and Cry1Fb, respectively, were created. In this way Cry1Ca, Cry1Fb, and to a lesser extent Cry1Ba were made considerably more toxic. 2004 Elsevier Inc. All rights reserved

The power of seaweeds as plant biostimulants to boost crop production under abiotic stress

Abiotic stresses like drought and salinity are major factors resulting in crop yield losses and soil degradation worldwide. To meet increasing food demands, we must improve crop productivity, especially under increasing abiotic stresses due to climate change. Recent studies suggest that seaweed-based biostimulants could be a solution to this problem. Here, we summarize the current findings of using these biostimulants and highlight current knowledge gaps. Seaweed extracts were shown to enhance nutrient uptake and improve growth performance in crops under stressed and normal conditions. Seaweed extracts contain several active compounds, for example, polysaccharides, polyphenols and phytohormones. Although some of these compounds have growth-promoting properties on plants, the molecular mechanisms that underly seaweed extract action remain understudied. In this paper, we review the role of these extracts and their bioactive compounds as plant biostimulants. The targeted application of seaweed extract to improve crop performance and protein accumulation is also discussed

In Vivo Hexamerization and Characterization of the Arabidopsis AAA ATPase CDC48A Complex Using Förster Resonance Energy Transfer-Fluorescence Lifetime Imaging Microscopy and Fluorescence Correlation Spectroscopy1[W][OA]

The Arabidopsis (Arabidopsis thaliana) AAA ATPase CDC48A was fused to cerulean fluorescent protein and yellow fluorescent protein. AAA ATPases like CDC48 are only active in hexameric form. Förster resonance energy transfer-based fluorescence lifetime imaging microscopy using CDC48A-cerulean fluorescent protein and CDC48A-yellow fluorescent protein showed interaction between two adjacent protomers, demonstrating homo-oligomerization occurs in living plant cells. Interaction between CDC48A and the SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 (SERK1) transmembrane receptor occurs in very restricted domains at the plasma membrane. In these domains the predominant form of the fluorescently tagged CDC48A protein is a hexamer, suggesting that SERK1 is associated with the active form of CDC48A in vivo. SERK1 trans-phosphorylates CDC48A on Ser-41. Förster resonance energy transfer-fluorescence lifetime imaging microscopy was used to show that in vivo the C-terminal domains of CDC48A stay in close proximity. Employing fluorescence correlation spectroscopy, it was shown that CDC48A hexamers are part of larger complexes

Cell plate-restricted association of Arabidopsis dynamin related proteins and PIN auxin efflux carriers is required for PIN endocytic trafficking during cytokinesis.

The polarized transport of the phytohormone auxin [1], which is crucial for the regulation of different stages of plant development [ [2] and [3] ], depends on the asymmetric plasma membrane distribution of the PIN-FORMED (PIN) auxin efflux carriers [4 A. Vieten, M. Sauer, P.B. Brewer and J. Friml, Molecular and cellular aspects of auxin-transport-mediated development. Trends Plant Sci., 12 (2007), pp. 160–168. Article | PDF (558 K) | | View Record in Scopus | | Cited By in Scopus (102) [4] and [5] ]. The PIN polar localization results from clathrin-mediated endocytosis (CME) from the plasma membrane and subsequent polar recycling [6]. The Arabidopsis genome encodes two groups of dynamin-related proteins (DRPs) that show homology to mammalian dynamin—a protein required for fission of endocytic vesicles during CME [ [7] and [8] ]. Here we show by coimmunoprecipitation (coIP), bimolecular fluorescence complementation (BiFC), and Förster resonance energy transfer (FRET) that members of the DRP1 group closely associate with PIN proteins at the cell plate. Localization and phenotypic analysis of novel drp1 mutants revealed a requirement for DRP1 function in correct PIN distribution and in auxin-mediated development. We propose that rapid and specific internalization of PIN proteins mediated by the DRP1 proteins and the associated CME machinery from the cell plate membranes during cytokinesis is an important mechanism for proper polar PIN positioning in interphase cells