Binding MyoD transcription factor

Figure 10.24 Structure of a monomer of the DNA-binding domain of the transcription factor MyoD. The domain, which belongs to the b/HLH family, comprises two a helices joined by a loop region. The basic region (blue) and the first helix HI (red) of the helix-loop-helLx region form one continous a helix. (Adapted from P.C.M. Ma et al.. Cell 77 451-459, 1994.)...

Figure 10.28 Schematic diagram of the binding of the transcription factor Max to DNA. The two monomers of Max (blue and green) form a dimer through both the helix-loop-helLx regions which form a four-helix bundle like MyoD, and the zipper regions, which are arranged in a coiled coil. The N-terminal basic regions bind to DNA in a way similar to GCN4 and MyoD. (Adapted from A.R. Ferre-D Amare et al., Nature 363 38-4S, 1993.)...

Carell has recently presented the study of a flavin amino acid chimera to model riboflavin in DNA photolyases [68]. This amino acid LI (Fig. 20) was synthesized in an enantiopure fashion by building the alloxazine ring onto the epsilon amine of lysine. This coenzyme chimera was applied to the problem of repairing DNA damage caused by UV irradiation. LI was incorporated into an 21-residue peptide, P-1, possessing the sequence of the DNA-binding domain of the helix-loop-helix transcription factor MyoD. 

Through the experiments on C3H lOTl/2 cells treated with 5-azacytidine, MyoD was identified as a key transcription factor in regulating the differentiation of muscle. To what general class of DNA-binding proteins does MyoD belong How do the interactions of MyoD with the following proteins affect its function (a) E2A, (b) MEFs, (c) Id... 

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