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C Crone J Frokjaer-Jensen JJ Friedman O Christensen 《The Journal of general physiology》1978,71(2):195-220
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Gonzalez-Bashan LE Lebsky VK Hernandez JP Bustillos JJ Bashan Y 《Canadian journal of microbiology》2000,46(7):653-659
In an agroindustrial wastewater pond, a naturally occurring unicellular microalga, Chlorella vulgaris, was closely associated with the terrestrial plant-associative N2-fixing bacterium Phyllobacterium myrsinacearum. When the two microorganisms were artificially coimmobilized in alginate beads, they shared the same internal bead cavities, and the production of five microalgal pigments increased, but there were no effects on the number of the cells or the biomass of the microalga. The association, however, reduces the ability of C. vulgaris to remove ammonium ions and phosphorus from water. The bacterium produced nitrate from ammonium in synthetic wastewater with or without the presence of the microalga, and fixed nitrogen in two culture media. Our results suggest that interactions between microalgae and associative bacteria should be considered when cultivating microalgae for wastewater treatment. 相似文献
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Lipoteichoic acid is an important microbe-associated molecular pattern of Lactobacillus rhamnosus GG
Claes Ingmar JJ Segers Marijke E Verhoeven Tine LA Dusselier Michiel Sels Bert F De Keersmaecker Sigrid CJ Vanderleyden Jos Lebeer Sarah 《Microbial cell factories》2012,11(1):1-8
Background
Receptors with a single transmembrane (TM) domain are essential for the signal transduction across the cell membrane. NMR spectroscopy is a powerful tool to study structure of the single TM domain. The expression and purification of a TM domain in Escherichia coli (E.coli) is challenging due to its small molecular weight. Although ketosteroid isomerase (KSI) is a commonly used affinity tag for expression and purification of short peptides, KSI tag needs to be removed with the toxic reagent cyanogen bromide (CNBr).Result
The purification of the TM domain of p75 neurotrophin receptor using a KSI tag with the introduction of a thrombin cleavage site is described herein. The recombinant fusion protein was refolded into micelles and was cleaved with thrombin. Studies showed that purified protein could be used for structural study using NMR spectroscopy.Conclusions
These results provide another strategy for obtaining a single TM domain for structural studies without using toxic chemical digestion or acid to remove the fusion tag. The purified TM domain of p75 neurotrophin receptor will be useful for structural studies. 相似文献10.