Biodegradation of Carbazole and Dibenzothiophene by Bacteria Isolated from Petroleum-Contaminated Sites

This study reports the isolation of bacterial cultures, capable of selective removal of nitrogen and sulfur from carbazole and dibenzothiophene, respectively. The isolates utilizing carbazole were found to be suitable for biorefining. These were designated as P10 and P11, and were identified as Pseudomonas sp. Growing cells of P10 and P11 could utilize 77% carbazole in 250 and 120 h, respectively. Isolates showing utilization of dibenzothiophene were not suitable for biorefining industry. Results suggest these Pseudomonas isolates may be useful in petroleum biorefining for the selective removal of organically bound nitrogen from petroleum.     

A modular approach for high-flux lactic acid production from methane in an industrial medium using engineered Methylomicrobium buryatense 5GB1

Journal of Industrial Microbiology & Biotechnology - Convergence of market drivers such as abundant availability of inexpensive natural gas and increasing awareness of its global warming...     

Optimization of Multimode Fibers for Surface Plasmon Resonance Based Sensors Under Spectral and Single Wavelength Intensity Interrogation

Plasmonics - In an optical fiber based SPR sensor, a segment of metal clad silica fiber is used as the sensing element and resonant coupling occurs to the surface plasmon mode excited at the...     

Anticipation of Antigenic Sites for the Goal of Vaccine Designing Against Nipah Virus: An Immunoinformatics Inquisitive Quest

International Journal of Peptide Research and Therapeutics - With time, the Nipah virus has been proved as a fatal and dangerous pathogen for humanity. Nipah virus has its origin from bats and...     

DNA recognition by Escherichia coli CbpA protein requires a conserved arginine–minor-groove interaction

Curved DNA binding protein A (CbpA) is a co-chaperone and nucleoid associated DNA binding protein conserved in most γ-proteobacteria. Best studied in Escherichia coli, CbpA accumulates to >2500 copies per cell during periods of starvation and forms aggregates with DNA. However, the molecular basis for DNA binding is unknown; CbpA lacks motifs found in other bacterial DNA binding proteins. Here, we have used a combination of genetics and biochemistry to elucidate the mechanism of DNA recognition by CbpA. We show that CbpA interacts with the DNA minor groove. This interaction requires a highly conserved arginine side chain. Substitution of this residue, R116, with alanine, specifically disrupts DNA binding by CbpA, and its homologues from other bacteria, whilst not affecting other CbpA activities. The intracellular distribution of CbpA alters dramatically when DNA binding is negated. Hence, we provide a direct link between DNA binding and the behaviour of CbpA in cells.