The University of Southampton
University of Southampton Institutional Repository

Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate

Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate
Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate
We have prepared a novel footprinting substrate which contains all 136 tetranucleotide sequences and have used this to determine the preferred binding sites for the synthetic quinoxaline antibiotic [N-MeCys3,N-MeCys7]TANDEM. We find that, although the ligand binds to all TpA steps, it binds best to the tetranucleotide sequence ATAT and shows only weak interaction with TTAA and GTAC. The best binding sites contain the sequences ATAX and XTAT.
footprinting, TANDEM, DNase I, quinoxaline antibiotic
0003-2697
246-250
Lavesa, M.
f3720d36-5310-4826-830e-28173e520472
Fox, K.R.
9da5debc-4e45-473e-ab8c-550d1104659f
Lavesa, M.
f3720d36-5310-4826-830e-28173e520472
Fox, K.R.
9da5debc-4e45-473e-ab8c-550d1104659f

Lavesa, M. and Fox, K.R. (2001) Preferred binding sites for [N-MeCys(3),N-MeCys(7)]TANDEM determined using a universal footprinting substrate. Analytical Biochemistry, 293 (2), 246-250. (doi:10.1006/abio.2001.5124).

Record type: Article

Abstract

We have prepared a novel footprinting substrate which contains all 136 tetranucleotide sequences and have used this to determine the preferred binding sites for the synthetic quinoxaline antibiotic [N-MeCys3,N-MeCys7]TANDEM. We find that, although the ligand binds to all TpA steps, it binds best to the tetranucleotide sequence ATAT and shows only weak interaction with TTAA and GTAC. The best binding sites contain the sequences ATAX and XTAT.

This record has no associated files available for download.

More information

Submitted date: 17 January 2001
Published date: 1 June 2001
Keywords: footprinting, TANDEM, DNase I, quinoxaline antibiotic

Identifiers

Local EPrints ID: 55960
URI: http://eprints.soton.ac.uk/id/eprint/55960
ISSN: 0003-2697
PURE UUID: e1a60144-1814-4a92-ad30-2f38f0fd00f7
ORCID for K.R. Fox: ORCID iD orcid.org/0000-0002-2925-7315

Catalogue record

Date deposited: 06 Aug 2008
Last modified: 16 Mar 2024 02:36

Export record

Altmetrics

Contributors

Author: M. Lavesa
Author: K.R. Fox ORCID iD

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×