Endophytic bacterium CIMAP-A7 mediated amelioration of atrazine induced phyto-toxicity in Andrographis paniculata.

The presence of atrazine, a triazine herbicide, and its residues in agriculture soil poses a serious threat to human health and environment through accumulation in edible plant parts. Hence, the present study focused on atrazine induced stress amelioration of Andrographis paniculata, an important medicinal plant, by a plant growth promoting and atrazine degrading endophytic bacterium CIMAP-A7 inoculation. Atrazine has a non-significant effect at a lower dose while at a higher dose (lower: 25 and higher: 50 mg kg-1) 22 and 36% decrease in secondary metabolite content and plant dry weight of A. paniculata was recorded, respectively. Endophyte CIMAP-A7 inoculation significantly reduced atrazine soil content, by 78 and 51% at lower and a higher doses respectively, than their respective control treatments. Inoculation of CIMAP-A7 exhibited better plant growth in terms of increased total chlorophyll, carotenoid, protein, and metabolite content with reduced atrazine content under both atrazine contaminated and un-contaminated treatments. Atrazine induced oxidative stress in A. paniculata was also ameliorated by CIMAP-A7 by reducing stress enzymes, proline, and malondialdehyde accumulation under contaminated soil conditions than un-inoculated treatments. Furthermore, the presence of atrazine metabolites deisopropylatrazine (DIA) and desethylatrazine (DEA) strongly suggests a role of CIMAP-A7 in mineralization however, the absence of these metabolites in uninoculated soil and all plant samples were recorded. These findings advocate that the amelioration of atrazine induced stress with no/least pesticide content in plant tissues by plant-endophyte co-interactions would be efficient in the remediation of atrazine contaminated soils and ensure safe crop produce.

Expression of CspE by a psychrotrophic bacterium Enterobacter ludwigii PAS1, isolated from Indian Himalayan soil and in silico protein modelling, prediction of conserved residues and active sites.

Proteome analysis of Enterobacter ludwigii PAS1 provide a powerful set of tool to study the cold shock proteins along with that combination of bioinformatics is useful for interpretation of comparative results from many species. There is a considerable interest in the use of psychrotrophic bacteria for nitrogen fixation, especially at hilly regions, thus better understanding of cold adaptation mechanisms too. The psychrotrophic E. ludwigii PAS1 grown at 30 and 4 °C, isolated from Himalaya soil was undertaken for proteomic responses during optimal and cold shock conditions. Comparative proteomic analyses using two-dimensional gel electrophoresis (2-DE) and MALDI-TOF/TOF MS revealed the presence of Cold shock protein E (CspE). Three-dimensional structure of CspE of E. ludwigii PAS1 divulge the presence of five antiparallel ß-sheets forming a ß-barrel structure with surface exposed aromatic and basic residues that were responsible for nucleic acid binding and also reveals the presence of highly conserved nucleic acid-binding motifs RNP1 and RNP2 in Csp family.