Difference between revisions of "Part:BBa K1442031"
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| − | + | The split neomycin system consists of both neo-α and neo-β. Neomycin confers kanamycin and geneticin resistance in ''E. coli'' and eukaryotic cells, respectively. The split neomycin system has been previously used in Schmidt et al., 2012. Traditionally, antibiotic selection of bacteria is performed with a single antibiotic resistance gene encoded within a single plasmid. If multiple plasmids are introduced into a bacteria, multiple antibiotics are required to select for successful transformants. In addition, the use of multiple antibiotics for selection also stresses the bacteria, which can reduce transformation efficiency. | |
| − | + | The split neomycin system overcomes these limitations, by having the α and β subunits encoded on two separate plasmids. Antibiotic resistance is only conferred following heterodimerization of the α and β subunit. Heterodimerization is mediated by leucine zippers, which, as the name implies acts as a zip that joins both the α and β subunits together. This part is useful for the synthetic biology community, as it can save on costs in respect to the purchase of multiple antibiotics. | |
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Revision as of 22:30, 29 October 2014
Split Neomycin
The split neomycin system consists of both neo-α and neo-β. Neomycin confers kanamycin and geneticin resistance in E. coli and eukaryotic cells, respectively. The split neomycin system has been previously used in Schmidt et al., 2012. Traditionally, antibiotic selection of bacteria is performed with a single antibiotic resistance gene encoded within a single plasmid. If multiple plasmids are introduced into a bacteria, multiple antibiotics are required to select for successful transformants. In addition, the use of multiple antibiotics for selection also stresses the bacteria, which can reduce transformation efficiency.
The split neomycin system overcomes these limitations, by having the α and β subunits encoded on two separate plasmids. Antibiotic resistance is only conferred following heterodimerization of the α and β subunit. Heterodimerization is mediated by leucine zippers, which, as the name implies acts as a zip that joins both the α and β subunits together. This part is useful for the synthetic biology community, as it can save on costs in respect to the purchase of multiple antibiotics.