ACC Deaminase-Containing Bacillus subtilis Reduces Stress Ethylene-Induced Damage and Improves Mycorrhizal Colonization and Rhizobial Nodulation in Trigonella foenum-graecum Under Drought Stress

This study was aimed at protecting Trigonella plants by reducing stress ethylene levels through ACC (1-aminocyclopropane-1-carboxylic acid) deaminase-containing Bacillus subtilis (LDR2) and promoting plant growth through improved colonization of beneficial microbes like Ensifer meliloti (Em) and Rhizophagus irregularis (Ri) under drought stress. A plant growth-promoting rhizobacterium strain possessing high levels of ACC deaminase characterized as B. subtilis was selected. Application of this strain considerably protected Trigonella plants under severe drought stress conditions; this protection was correlated with reduced levels of ACC (responsible for generation of stress ethylene). The experiment consisted of eight inoculation treatments with different combinations of ACC deaminase-containing rhizobacteria LDR2, Ri, and Em under three water regimes. The tripartite combination of LDR2 + Ri + Em acted synergistically to induce protective mechanisms against decreased soil water availability in Trigonella plants and improved plant weight by 56 % with lower ACC concentration (39 % less than stressed noninoculated plants) under severe drought conditions. Drought-induced changes in biochemical markers like reduced chlorophyll concentration, increased proline content, and higher lipid peroxidation were monitored and clearly indicated the protective effects of LDR2 under drought stress. Under drought conditions, apart from alleviating ethylene-induced damage, LDR2 enhanced nodulation and arbuscular mycorrhizal fungi colonization in the plants resulting in improved nutrient uptake and plant growth.     

Zinc – An Indispensable Micronutrient

Availability of Zn to plant is hampered by its immobile nature and adverse soil conditions. Thus, Zn deficiency is observed even though high amount is available in soil. Root-shoot barrier, a major controller of zinc transport in plant is highly affected by changes in the anatomical structure of conducting tissue and adverse soil conditions like pH, clay content, calcium carbonate content, etc. Zn deficiency results in severe yield losses and in acute cases plant death. Zn deficiency in edible plant parts results in micronutrient malnutrition leading to stunted growth and improper sexual development in humans. To overcome this problem several strategies have been used to enrich Zn availability in edible plant parts, including nutrient management, biotechnological tools, and classical and molecular breeding approaches.     

Is the fracto‐mechanoluminescence of ZnS:Mn phosphor dominated by charged dislocation mechanism or piezoelectrification mechanism?

Mathematical approaches made for both the charged dislocation model and piezoelectrically induced electron bombardment model of fracto‐mechanoluminescence (FML), the luminescence induced by fracture of solids, in ZnS:Mn phosphor indicate that the piezoelectrically induced electron bombardment model provides a dominating process for the FML of ZnS phosphors. The concentration of 3000 ppm Mn²⁺ is optimal for ML intensity of ZnS:Mn phosphor. The decay time of ML gives the relaxation time of the piston used to deform the sample and the time t_m of maximum of ML is controlled by both the relaxation time of the piston and decay time of charges on the newly created surfaces of crystals. As the product of the velocity of dislocations and pinning time of dislocations gives the mean free path of a moving dislocation. Both factors play an important role in the ML excitation of impurity doped II–VI semiconductors. The linear increase of total ML intensity I_T with the impact velocity indicates that the damage increases linearly with impact velocity of the load. Thus, the ML measurement can be used remotely to monitor the real‐time damage in the structures, and therefore, the ML of ZnS:Mn phosphor has also the potential for a structural health monitoring system. Copyright © 2015 John Wiley & Sons, Ltd.     

Development of a non-linear growth model for predicting temporal evolution of Scenedesmus obliquus with varying irradiance

Bioprocess and Biosystems Engineering - In the present study, the effect of irradiance on growth performance of Scenedesmus obliquus was investigated, and various non-linear growth models were...     

Nod1-mediated lipolysis promotes diacylglycerol accumulation and successive inflammation via PKCδ-IRAK axis in adipocytes

Chronic inflammation contributes to obesity mediated metabolic disturbances, including insulin resistance. Obesity is associated with altered microbial load in metabolic tissues that can contribute to metabolic inflammation. Different bacterial components such as, LPS, peptidoglycans have been shown to underpin metabolic disturbances through interaction with host innate immune receptors. Activation of Nucleotide-binding oligomerization domain-containing protein 1 (Nod1) with specific peptidoglycan moieties promotes insulin resistance, inflammation and lipolysis in adipocytes. However, it was not clear how Nod1-mediated lipolysis and inflammation is linked. Here, we tested if Nod1-mediated lipolysis caused accumulation of lipid intermediates and promoted cell autonomous inflammation in adipocytes. We showed that Nod1-mediated lipolysis caused accumulation of diacylglycerol (DAG) and activation of PKCδ in 3T3-L1 adipocytes, which was prevented with a Nod1 inhibitor. Nod1-activated PKCδ caused downstream stimulation of IRAK1/4 and was associated with increased expression of proinflammatory cytokines such as, IL-1β, IL-18, IL-6, TNFα and MCP-1. Pharmacological inhibition or siRNA mediated knockdown of IRAK1/4 attenuated Nod1-mediated activation of NF-κB, JNK, and the expression of proinflammatory cytokines. These results reveal that Nod1-mediated lipolysis promoted accumulation of DAG, which engaged PKCδ and IRAK1/4 to augment inflammation in 3T3-L1 adipocytes.     

Active site geometry of oxalate decarboxylase from Flammulina velutipes: Role of histidine-coordinated manganese in substrate recognition

Oxalate decarboxylase (OXDC) from the wood-rotting fungus Flammulina velutipes, which catalyzes the conversion of oxalate to formic acid and CO(2) in a single-step reaction, is a duplicated double-domain germin family enzyme. It has agricultural as well as therapeutic importance. We reported earlier the purification and molecular cloning of OXDC. Knowledge-based modeling of the enzyme reveals a beta-barrel core in each of the two domains organized in the hexameric state. A cluster of three histidines suitably juxtaposed to coordinate a divalent metal ion exists in both the domains. Involvement of the two histidine clusters in the catalytic mechanism of the enzyme, possibly through coordination of a metal cofactor, has been hypothesized because all histidine knockout mutants showed total loss of decarboxylase activity. The atomic absorption spectroscopy analysis showed that OXDC contains Mn(2+) at up to 2.5 atoms per subunit. Docking of the oxalate in the active site indicates a similar electrostatic environment around the substrate-binding site in the two domains. We suggest that the histidine coordinated manganese is critical for substrate recognition and is directly involved in the catalysis of the enzyme.     

Plasticity in structure and interactions is critical for the action of indolicidin,an antibacterial peptide of innate immune origin

The comparative analysis of two cationic antibacterial peptides of the cathelicidin family-indolicidin and tritrypticin-enabled addressing the structural features critical for the mechanism of indolicidin activity. Functional behavior of retro-indolicidin was found to be identical to that of native indolicidin. It is apparent that the gross conformational propensities associated with retro-peptides resemble those of the native sequences, suggesting that native and retro-peptides can have similar structures. Both the native and the retro-indolicidin show identical affinities while binding to endotoxin, the initial event associated with the antibacterial activity of cationic peptide antibiotics. The indolicidin-endotoxin binding was modeled by docking the indolicidin molecule in the endotoxin structure. The conformational flexibility associated with the indolicidin residues, as well as that of the fatty acid chains of endotoxin combined with the relatively strong structural interactions, such as ionic and hydrophobic, provide the basis for the endotoxin-peptide recognition. Thus, the key feature of the recognition between the cationic antibacterial peptides and endotoxin is the plasticity of molecular interactions, which may have been designed for the purpose of maintaining activity against a broad range of organisms, a hallmark of primitive host defense.