4 results match your criteria: "Ben-Gurion University of the Negevgrid.7489.2[Affiliation]"
mSystems
August 2022
Newe Ya'ar Research Center, Agricultural Research Organizationgrid.410498.0, Ramat Yishay, Israel.
Extensive use of agrochemicals is emerging as a serious environmental issue coming at the cost of the pollution of soil and water resources. Bioremediation techniques such as biostimulation are promising strategies used to remove pollutants from agricultural soils by supporting the indigenous microbial degraders. Though considered cost-effective and eco-friendly, the success rate of these strategies typically varies, and consequently, they are rarely integrated into commercial agricultural practices.
View Article and Find Full Text PDFMicrobiol Spectr
August 2022
Israel Oceanographic and Limnological Researchgrid.419264.c, The National Center for Mariculture, Eilat, Israel.
Halotolerant bacteria capable of starch hydrolysis by their amylases will benefit various industries, specifically since the hydrolytic activity of current industrial amylases is inhibited or even absent in salt-rich or alkaline environments. Seeking novel enzymes, we analyzed the entire genome content of a marine bacterium isolated from the gut of sea urchins to compare it against other bacterial genomes. Conditions underlying α-amylase activity were examined at various salinities (0 to 4%) and temperatures (25°C to 37°C).
View Article and Find Full Text PDFJ Bacteriol
January 2022
Department of Life Sciences, Ben-Gurion University of the Negevgrid.7489.2, Beersheva, Israel.
Haloferax volcanii AglD is currently the only archaeal dolichol phosphate (DolP)-mannose synthase shown to participate in N-glycosylation. However, the relation between AglD and Pyrococcus furiosus PF0058, the only archaeal DolP-mannose synthase for which structural information is presently available, was unclear. In this report, similarities between the PF0058 and AglD catalytic domains were revealed.
View Article and Find Full Text PDFmBio
August 2021
Department of Life Sciences, Ben-Gurion University of the Negevgrid.7489.2, Beer-Sheva, Israel.
-Adenosylmethionine lyase (SAMase) of bacteriophage T3 degrades the intracellular SAM pools of the host Escherichia coli cells, thereby inactivating a crucial metabolite involved in a plethora of cellular functions, including DNA methylation. SAMase is the first viral protein expressed upon infection, and its activity prevents methylation of the T3 genome. Maintenance of the phage genome in a fully unmethylated state has a profound effect on the infection strategy.
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