Basic helix-loop-helix protein MyoD displays modest DNA binding specificity

Künne, A, Meierhans, D. and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 1996. Basic helix-loop-helix protein MyoD displays modest DNA binding specificity. FEBS Letters 391 (1-2) , pp. 79-83. 10.1016/0014-5793(96)00707-7

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Abstract

The expression of MyoD can activate muscle specific genes and myogenic differentiation in many cell types. The hypothesis that the DNA binding specificity of MyoD is responsible for its biological specificity was tested. Homodimers of MyoD bind to E-box containing DNA with high affinity, but do not form stable and well defined complexes with heterologous DNA sequences. The physiologically active heterodimer of MyoD and E12 binds an oligonucleotide containing an E-box sequence with an affinity only two orders of magnitude higher than a completely unrelated DNA sequence, stressing the importance of cooperative interactions with other proteins of the transcriptional machinery for specific gene activation.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry Cardiff Catalysis Institute (CCI)
Subjects:	Q Science > QD Chemistry
Uncontrolled Keywords:	Transcription factor; Protein-DNA interaction; Gene expression; Specificity; Protein-protein interaction
Publisher:	Elsevier
ISSN:	0014-5793
Last Modified:	18 Oct 2022 13:19
URI:	https://orca.cardiff.ac.uk/id/eprint/13458

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