Rice (Oryza sativa L.) plant growth and productivity is adversely affected by various stress factors. Overexpression of drought tolerance‐related genes is one of the best approaches for developing drought‐resistant transgenics. Agrobacterium tumefaciens has been widely used in generating transgenic plants through plasmid vector to obtain desired characteristics and to know the specific expression profiles of genes in the plant. The enhancer trap method was developed to know the specific expression of genes at different stages of growth by entrapping the genes of an organism. In the present study, we designed a vector molecule with a feature of promoting the expression of a specific gene more than four times than its normal expression and it is useful for efficient transformation to higher plants by utilizing the trans configuration of vir genes of the plasmid A. tumefaciens, to transfer right and left sequence bordered of transferred DNA (T‐DNA) into the nuclear genome of plants. We developed a binary vector consisting of 1.8‐kb green fluorescent protein (GFP) cassette as a reporter gene and 1.4‐kb tetramer of CaMv35S enhancer (4XEn) were cloned at HindIII site of pSB11 bar intermediate vector to tag and know the genes and their expression profiles, then mobilized into A. tumefaciens to produce a super‐binary vector pSB111‐bar‐4XEn‐GFP. The resultant construct was confirmed by polymerase chain reaction and restriction digestion methods. Finally, we discuss the role of overexpressed ascorbate peroxidase in drought stress.

Cell wall proteins from Neurospora crassa were isolated and evaluated to demonstrate their metal ability to bind Ca 2+ /Sr 2+ by loading the solubilized protein fraction on to immobilized metal affinity chromatography (IMAC) column pre-equilibrated with Ca 2+ /Sr 2+ . The sodium dodecyl sulfatepolyacrylamide gel electrophoresis analysis IMAC eluent, revealed ∼18 proteins with a similarity in the proteome pattern of Ca 2+ /Sr 2+ fractions.Diethyl aminoethyl chromatography showed five proteins in common in binding to Ca 2+ and Sr 2+ , were subjected to N-terminal sequencing. The sequence analysis was studied for the determination of metal-binding site prediction by CHED software indicating that all five were found to have a high affinity toward Ca 2+ . From these five, two were randomly selected and denoted as CWP-A (possess five Ca binding sites of six metal-binding sites) and CWP-B (possess six binding sites of eight metal-binding sites). They were selected for further characterization studies to determine their Ca 2+ bound Sr 2+ binding properties. Surprisingly, these proteins were able to bind Sr 2+ ions (29 μmol) with equal affinity as to Ca 2+ ions (42 μmol) by means of direct binding, and/or by displacing calcium as observed in metal-dependent proteolytic protection, fluorescence-based metal exchange assays, and molecular simulation studies. From the results, we demonstrate for the first time, that there is a stoichiometry between Ca 2+ (an essential macro elemental metal ion) and Sr 2+ ions (a nonessential element for which no reported metabolic activity is reported) for the metal-binding sites on cell wall proteins.