Expression,purification and characterization of UvrD2 helicase from Mycobacterium tuberculosis |
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| Authors: | Konstantin Kazarian Camilla Cassani Menico Rizzi |
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| Institution: | 1. Department of Chemical and Pharmaceutical Sciences, University of Trieste, P.zle Europa 1, 34127 Trieste, Italy;2. Department of Drug Sciences, University of Pavia, Via Taramelli 12, Pavia, Italy;3. Center for Studies and Researches in Ethno Pharmacy (C.I.St.R.E.), University of Pavia, Via Taramelli 12, 27100 Pavia, Italy;3. Department of Infection, Immunity and Inflammation, University of Leicester, Leicester LE1 9HN, United Kingdom,;4. Brighton and Sussex Medical School, University of Sussex, Brighton BN1 9PX, United Kingdom,;5. Medical Microbiology, Centre for Infection and Immunity, Division of Clinical Sciences, St. George''s University of London, London SW17 0RE, United Kingdom,;6. Centre de Biochimie Structurale, CNRS UMR 5048, 34090 Montpellier, France,;12. Institute of Biological, Environmental and Rural Sciences, Aberystwyth University, Aberystwyth SY23 3DD, United Kingdom;1. Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 15000, PR China;2. School of Medicine, Tsinghua University, Beijing 100084, PR China;3. Fujian Agriculture and Forestry University, Fuzhou 350002, PR China |
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| Abstract: | Helicases appear to be important for genome stability of dormant Mycobacterium tuberculosis responsible for latent tuberculosis infection and big proportion of active disease cases caused by reactivation. It was demonstrated that in both M. tuberculosis and Mycobacterium smegmatis, a helicase termed UvrD2 is essential for bacterial growth making it a promising target to fight tuberculosis. In many cases expression of soluble and active mycobacterial proteins in Escherichia coli is a complicated issue. In this work we for the first time report a non-trivial expression procedure in E. coli, leading to soluble UvrD2 from M. tuberculosis which possesses DNA-dependent ATP-ase activity. |
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