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

FEBS Letters

Künne, Andreas G.E.¹  Meierhans, Daniel¹  Allemann, Rudolf K.¹ 

[1] Department of Chemistry, ETH-Zurich, Universitätstrasse 16, CH-8092 Zurich, Switzerland

关键词: Transcription factor;    Protein-DNA interaction;    Gene expression;    Specificity;    Protein-protein interaction;    BHLH;    basic-helix-loop-helix;    CASTing;    cyclic amplification and selection of targets;    CD;    circular dichroism;    EMSA;    electrophoretic mobility shift assay;    HPLC;    high performance liquid chromatography;    MCK;    muscle creatine kinase;    SAAB;    selected and amplified binding site ‘imprints’;   

DOI  :  10.1016/0014-5793(96)00707-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown