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 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

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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:	18 Oct 2022 13:19
URI:	https://orca.cardiff.ac.uk/id/eprint/13479

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