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Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE

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Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE. / Boxer, David H.; Zhang, Han; Gourley, David G.; Hunter, William N.; Kelly, Sharon M.; Price, Nicholas C.

In: Organic and Biomolecular Chemistry, Vol. 2, No. 19, 2004, p. 2829-2837.

Research output: Contribution to journalArticle

Harvard

Boxer, DH, Zhang, H, Gourley, DG, Hunter, WN, Kelly, SM & Price, NC 2004, 'Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE' Organic and Biomolecular Chemistry, vol 2, no. 19, pp. 2829-2837., 10.1039/B404185B

APA

Boxer, D. H., Zhang, H., Gourley, D. G., Hunter, W. N., Kelly, S. M., & Price, N. C. (2004). Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE. Organic and Biomolecular Chemistry, 2(19), 2829-2837. 10.1039/B404185B

Vancouver

Boxer DH, Zhang H, Gourley DG, Hunter WN, Kelly SM, Price NC. Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE. Organic and Biomolecular Chemistry. 2004;2(19):2829-2837. Available from: 10.1039/B404185B

Author

Boxer, David H.; Zhang, Han; Gourley, David G.; Hunter, William N.; Kelly, Sharon M.; Price, Nicholas C. / Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE.

In: Organic and Biomolecular Chemistry, Vol. 2, No. 19, 2004, p. 2829-2837.

Research output: Contribution to journalArticle

Bibtex - Download

@article{3f970f7b219940638509b5edbc2b2012,
title = "Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE",
author = "Boxer, {David H.} and Han Zhang and Gourley, {David G.} and Hunter, {William N.} and Kelly, {Sharon M.} and Price, {Nicholas C.}",
note = "dc.publisher: Royal Society of Chemistry",
year = "2004",
doi = "10.1039/B404185B",
volume = "2",
number = "19",
pages = "2829--2837",
journal = "Organic and Biomolecular Chemistry",
issn = "1477-0520",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Sensing of remote oxyanion binding at the DNA binding domain of the molybdate-dependent transcriptional regulator, ModE

A1 - Boxer,David H.

A1 - Zhang,Han

A1 - Gourley,David G.

A1 - Hunter,William N.

A1 - Kelly,Sharon M.

A1 - Price,Nicholas C.

AU - Boxer,David H.

AU - Zhang,Han

AU - Gourley,David G.

AU - Hunter,William N.

AU - Kelly,Sharon M.

AU - Price,Nicholas C.

PY - 2004

Y1 - 2004

N2 - The molybdate-dependent transcriptional regulator ModE of Escherichia coli displays a large (50%) quenching of its intrinsic tryptophan fluorescence on binding molybdate. The changes in fluorescence have been exploited to analyse the binding of molybdate to ModE. Utilising site-directed mutagenesis, a series of phenylalanine substitutions for the three tryptophans of ModE (Trp49, Trp131 and Trp186) have been constructed, to yield three mono-Trp-containing derivatives. This has allowed an assessment to be made of the contribution of each of the three tryptophans to the spectral changes observed on binding molybdate; these are most distinctive for Trp186. Linkage between the DNA-binding and molybdate-binding sites (some 55 Å apart) is shown by (a) the small, but definite, effect of molybdate on the fluorescence of Trp49 which is located at the DNA-binding winged helix–turn–helix domain, and (b) the finding that the binding of either ligand is enhanced in the presence of the other. The studies demonstrate that the mono-Trp derivatives of ModE could be useful tools with which to study the signal transduction processes specifically associated with molybdate-dependent transcriptional regulation and that this approach may have wider implications for analysis of other regulated systems.

AB - The molybdate-dependent transcriptional regulator ModE of Escherichia coli displays a large (50%) quenching of its intrinsic tryptophan fluorescence on binding molybdate. The changes in fluorescence have been exploited to analyse the binding of molybdate to ModE. Utilising site-directed mutagenesis, a series of phenylalanine substitutions for the three tryptophans of ModE (Trp49, Trp131 and Trp186) have been constructed, to yield three mono-Trp-containing derivatives. This has allowed an assessment to be made of the contribution of each of the three tryptophans to the spectral changes observed on binding molybdate; these are most distinctive for Trp186. Linkage between the DNA-binding and molybdate-binding sites (some 55 Å apart) is shown by (a) the small, but definite, effect of molybdate on the fluorescence of Trp49 which is located at the DNA-binding winged helix–turn–helix domain, and (b) the finding that the binding of either ligand is enhanced in the presence of the other. The studies demonstrate that the mono-Trp derivatives of ModE could be useful tools with which to study the signal transduction processes specifically associated with molybdate-dependent transcriptional regulation and that this approach may have wider implications for analysis of other regulated systems.

U2 - 10.1039/B404185B

DO - 10.1039/B404185B

M1 - Article

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

SN - 1477-0520

IS - 19

VL - 2

SP - 2829

EP - 2837

ER -

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