Exploring Crop–Microbiome Interactions Towards Improving Symbiotic Performance of Chickpea (Cicer arietinum) Cultivars Using Cyanobacterial Inoculants

The significance of integrated nutrient management practices is well established in improving the productivity of chickpea (Cicer arietinum); however, the effects of the inoculation of cyanobacterial inoculants on nodule metabolism, microbiome and associated genes are less explored. In the present investigation, cyanobacterium Anabaena laxa (A. laxa) and biofilm developed using Anabaena torulosa, with Mesorhizobium ciceri as a partner (An-M. ciceri), were evaluated along with Mesorhizobium ciceri (M. ciceri) alone, in three chickpea cultivars. Microbial inoculation led to 40–70% enhancement in nitrogen fixation, leghaemoglobin and ureide content, and two- to threefold increment in nitrate reductase and phosphoenolpyruvate carboxylase activity of the nodules. An enhancement of 30–50% in the soil available macro- and micronutrients and plant growth attributes was also observed. A significant correlation between the soil microbiological and plant parameters was recorded, particularly in relation to the nitrogen dynamics. Increases in the leghaemoglobin content in nodules due to An-M. ciceri, A. laxa and M. ciceri ranged from 18 to 40%, particularly in chickpea cv. BG372 in which 60–80% enhancement was recorded. Whereas the nifH gene copies in the nodule tissues ranged from 5.00 × 10⁶ to 3.35 × 10⁷ g⁻¹, the application of A. laxa led to higher abundances of nifH gene copies in desi chickpea cv. BG372 and kabuli BG1053 cultivars. An-M. ciceri, followed closely by A. laxa, was the top-ranking treatment, and chickpea cv. BG372 was the best performing cultivar; An-M. ciceri—chickpea cv. BG372 proved to be the superior combination for higher plant growth and soil nutrient-related traits.

     

Poly(ε-L-lysine): Synthesis and conformation

The synthesis of poly(ε-L -lysine) is described. This is a poly(ε-amino acid) in which the ε-amino group of lysine is condensed with the α-carboxyl group to produce a chain backbone that is a variant of the usual one seen in proteins and the side chain is the α-amino group. Conformational studies of poly(ε-L -lysine) and its t-butyloxycarbonyl derivative suggest the likelihood of a chain order that is formally similar to the antiparallel pleated-sheet conformation of proteins.     

Quorum sensing inhibition as a promising method to control biofilm growth in metalworking fluids

Journal of Industrial Microbiology & Biotechnology - Microbial contamination in metalworking systems is a critical problem. This study determined the microbial communities in metalworking...     

Origins of life: conformational energy calculations on primitive tRNA nestling an amino acid

We report conformational energy calculations on our proposal of a molecular interaction theory for the origin of the nucleic acid-directed, adaptor-mediated synthesis of proteins that links the phenomena of chemical and biological evolution. A particular conformation of a pentanucleotide turns out to be a double-sided template for a primitive decoding system. It is able to neatly nestle an amino acid via hydrogen bonds, and this complex is found to be an energetically favourable conformation. The total potential energy of the complex is calculated using semi-empirical potential energy functions. A local-minimum conformation is obtained and its features are reported. The template conformation of the pentanucleotide is found to have an energy value far lower than a regular helical conformation. When the amino acid is nestled in the cleft of the template-conformation through specific hydrogen bonds, the energy is further lowered. A D-amino acid nestled into the PIT (Primitive tRNA) is found to be less stable than its L counterpart, as revealed by energy calculations.