Structural insights into the EthR–DNA interaction using native mass spectrometry

Daniel Shiu-Hin Chan; Wei-Guang Seetoh; Brendan N. McConnell; Dijana Matak-Vinković; Sherine E. Thomas; Vitor Mendes; Michal Blaszczyk; Anthony G. Coyne; Tom L. Blundell; Chris Abell

doi:10.1039/C7CC00804J

Structural insights into the EthR–DNA interaction using native mass spectrometry†

Daniel Shiu-Hin Chan,^a Wei-Guang Seetoh,

^a Brendan N. McConnell,

^a Dijana Matak-Vinković,^a Sherine E. Thomas,^b Vitor Mendes,

^b Michal Blaszczyk,^b Anthony G. Coyne,^a Tom L. Blundell^b and Chris Abell

*^a

Author affiliations

* Corresponding authors

^a Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, UK
E-mail: ca26@cam.ac.uk

^b Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK

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.

This article is part of the themed collections: In memory of Chris Abell and Celebrating our 2020 Prize and Award winners

Chemical Communications

Structural insights into the EthR–DNA interaction using native mass spectrometry†

Abstract

Supplementary files

Article information

Download Citation

Permissions

Structural insights into the EthR–DNA interaction using native mass spectrometry

Social activity

Search articles by author

Spotlight

Advertisements