Association of peptidyl prolyl cis/trans isomerase Rrd1 with C terminal domain of RNA polymerase II.

The largest subunit of RNAPII extends as the conserved unstructured heptapeptide consensus repeats YSPTSPS and their posttranslational modification, especially the phosphorylation state at Ser2, Ser5 and Ser7 of CTD recruits different transcription factors involved in transcription. In the current study, fluorescence anisotropy, pull down assay and molecular dynamics simulation studies employed to conclude that peptidyl-prolyl cis/trans-isomerase Rrd1 has strong affinity for unphosphorylated CTD rather than phosphorylated CTD for mRNA transcription. Rrd1 preferentially interacts with unphosphorylated GST-CTD in comparison to hyperphosphorylated GST-CTD in vitro.

Enhanced textile dye removal from wastewater using natural biosorbent and Shewanella algae B29: Application of Box Behnken design and genomic approach.

In this study, Box-Behnken design combining seven factors at three levels were used to optimize the elimination of CI Reactive Red 66 in artificial seawater, by the combination of eco-friendly bio-sorbents and acclimated halotolerant microbial strain. Results showed that macro-algae and cuttlebone (2 %) were the best natural bio-sorbent. Additionally, the selected halotolerant strain able to rapidly remove dye was identified as Shewanella algae B29.

Computational screening of natural compounds as putative quorum sensing inhibitors targeting drug resistance bacteria: Molecular docking and molecular dynamics simulations.

Quorum sensing (QS) is a bacterial communication strategy controlling cells density, biofilm formation, virulence, sporulation, and survival. Since QS is considered a virulence factor in drug-resistant pathogenic bacteria, inhibition of QS can contribute to control the spread of these bacteria. We propose in this study to test in silico, 19 natural compounds for their potential to inhibit QS transcriptional regulators of Pseudomonas aeruginosa (LasR and PqsE) and Chromobacterium violaceum (CviR and CviR').