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- W816171962 abstract "Conjugation is the transfer of DNA from a donor to a recipient bacterium through a DNA translocation channel known as a Type IV Secretion System (T4SS). Our work focuses on the T4SS of ICEBs1, the integrative and conjugative element found in Bacillus subtilis. ConE is a component of the ICEBs1 T4SS. ConE is a VirB4-like ATPase, most likely utilizing the energy generated from ATP hydrolysis for DNA transfer or T4SS assembly. Previously, we fused a hexa-histidine tag (His6) to ConE for ease of purification via nickel affinity chromatography. However, we found that surprisingly low concentrations of imidazole inadvertently wash His6-ConE off the nickel resin, preventing us from obtaining a high yield of pure protein. Here, we cloned deca-histidine tagged ConE (His10-ConE) and purified it side by side with His6-ConE. We observed that His10-ConE can be purified in higher yield and with fewer contaminants than His6-ConE. After optimization, we conducted a large-scale purification of His10-ConE for the purpose of obtaining antigen for production of antibodies to ConE. In the future, the antibodies will be used in western blots, pull-down assays, and immunofluorescence microscopy to characterize ConE levels, interactions, and localization, respectively. Additionally, we plan on exploring His10-ConE's ability to interact with DNA using electrophoretic mobility shift assays." @default.
- W816171962 created "2016-06-24" @default.
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- W816171962 date "2015-04-01" @default.
- W816171962 modified "2023-09-25" @default.
- W816171962 title "Purification and characterization of a bacterial mating protein" @default.
- W816171962 doi "https://doi.org/10.1096/fasebj.29.1_supplement.574.9" @default.
- W816171962 hasPublicationYear "2015" @default.
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