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Controlling the DNA Binding Specificity of bHLH Proteins through Intramolecular Interactions

Turner, Elizebeth C., Cureton, Charlotte H., Weston, Chris J., Smart, Oliver S. and Allemann, Rudolf Konrad 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

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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: Chemistry
Cardiff Catalysis Institute (CCI)
Subjects: Q Science > QD Chemistry
Publisher: Elsevier
ISSN: 1074-5521
Last Modified: 04 Jun 2017 02:54
URI: http://orca.cf.ac.uk/id/eprint/13479

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