Turner, Elizebeth C., Cureton, Charlotte H., Weston, Chris J., Smart, Oliver S. and Allemann, Rudolf Konrad  ORCID: https://orcid.org/0000-0002-1323-8830
2004.
Controlling the DNA Binding Specificity of bHLH Proteins through Intramolecular Interactions.
Chemistry & Biology
11
(1)
, pp. 69-77.
10.1016/j.chembiol.2003.12.015
|
Abstract
Reversible control of the conformation of proteins was employed to probe the relationship between flexibility and specificity of the basic helix-loop-helix protein MyoD. A fusion protein (apaMyoD) was designed where the basic DNA binding helix of MyoD was stablized by an amino-terminal extension with a sequence derived from the bee venom peptide apamin. The disulfide-stabilized helix from apamin served as a nucleus for a helix that extended for a further ten residues, thereby holding apaMyoD's DNA recognition helix in a predominantly α-helical conformation. The thermal stability of the DNA complexes of apaMyoD was increased by 13°C relative to MyoD-bHLH. Measurements of the fluorescence anisotropy change on DNA binding indicated that apaMyoD bound to E-box-containing DNA sequences with enhanced affinity relative to MyoD-bHLH. Consequently, the DNA binding specificity of apaMyoD was increased 10-fold.
| Item Type: | Article |
|---|---|
| Date Type: | Publication |
| Status: | Published |
| Schools: | Schools > Chemistry Research Institutes & Centres > Cardiff Catalysis Institute (CCI) |
| Subjects: | Q Science > QD Chemistry |
| Publisher: | Elsevier |
| ISSN: | 1074-5521 |
| Last Modified: | 18 Oct 2022 13:19 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/13479 |
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