Structural insights into the EthR-DNA interaction using native mass spectrometry
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Peer-reviewed
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Abstract
EthR is a transcriptional repressor that increases Mycobacterium tuberculosis resistance to ethionamide. In this study, the EthR-DNA interaction has been investigated by native electrospray-ionization mass spectrometry for the first time. The results show that up to six subunits of EthR are able to bind to its operator.
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Keywords
Calorimetry, DNA, Bacterial, Drug Resistance, Bacterial, Ethionamide, Mycobacterium tuberculosis, Spectrometry, Mass, Electrospray Ionization, Thermodynamics
Journal Title
Chemical Communications
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1359-7345
1364-548X
1364-548X
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Publisher
Royal Society of Chemistry
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Sponsorship
Wellcome Trust (090340/Z/09/Z)
Bill & Melinda Gates Foundation (via Foundation for the National Institutes of Health (FNIH)) (ABELL11HTB0)
Bill & Melinda Gates Foundation (via Foundation for the National Institutes of Health (FNIH)) (ABELL11HTB0)
D.S.-H. Chan acknowledges the support of the Croucher Foundation and the Cambridge Commonwealth, European and International Trust for receipt of a Croucher Cambridge International Scholarship. W.-G. Seetoh was supported by the Agency for Science, Technology and Research (A*STAR) Singapore (PhD sponsorship) and the Wellcome Trust Strategic Award (090340/Z/09/Z). B.N. McConnell acknowledges Cambridge Australia Scholarships for the award of a Poynton Scholarship, the Cambridge Philosophical Society and the Access to Learning Fund. S.E. Thomas is supported by the Cystic Fibrosis Trust. V. Mendes and M. Blaszczyk acknowledge the Bill & Melinda Gates Foundation (subcontract by the Foundation for the National Institutes of Health - NIH) (OPP1024021).