A cellular factor stimulates the DNA-binding activity of MyoD and E47.

We show that mixing purified MyoD and E47 proteins results in heterodimers that fail to bind DNA, even though MyoD and E47 homodimers can bind DNA efficiently. Addition of cell extracts or a specific fraction from a cell extract enables the heterodimer to bind DNA, but components in this fraction fail to enter the DNA complex. The activity is sensitive to heat and protease and is not ATP-dependent. The activity functions on E47 and MyoD homodimers and can stimulate DNA binding of the basic-helix-loop-helix region of MyoD. The effectiveness of the activity, for MyoD homodimers, depends on the exact DNA sequence of the binding site. Our results suggest that specific factors in the cell might control the DNA-binding properties of helix-loop-helix proteins.