Publication: Characterization and mutational analysis of the RecQ core of the bloom syndrome protein
Characterization and mutational analysis of the RecQ core of the bloom syndrome protein
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Janscak, P., Garcia, P. L., Hamburger, F., Makuta, Y., Shiraishi, K., Imai, Y., Ikeda, H., & Bickle, T. A. (2003). Characterization and mutational analysis of the RecQ core of the bloom syndrome protein. Journal of Molecular Biology, 330, 29–42. https://doi.org/10.1016/S0022-2836(03)00534-5
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Abstract
Bloom syndrome protein forms an oligomeric ring structure and belongs to a group of DNA helicases showing extensive homology to the Escherichia coli DNA helicase RecQ, a suppressor of illegitimate recombination. After over-production in E.coli, we have purified the RecQ core of BLM consisting of the DEAH, RecQ-Ct and HRDC domains (amino acid residues 642-1290). The BLM(642-1290) fragment could function as a DNA-stimulated ATPase and as a DNA helicase, displaying the same substrate specificity as the full-size protein. Gel-filtration e
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Janscak, P., Garcia, P. L., Hamburger, F., Makuta, Y., Shiraishi, K., Imai, Y., Ikeda, H., & Bickle, T. A. (2003). Characterization and mutational analysis of the RecQ core of the bloom syndrome protein. Journal of Molecular Biology, 330, 29–42. https://doi.org/10.1016/S0022-2836(03)00534-5