Ebneth A, Schweers O, Thole H, Fagin U, Urbanke C, Maass G, Wolfes H
Zentrum Biochemie, Medizinische Hochschule Hannover, Germany.
Biochemistry. 1994 Dec 6;33(48):14586-93. doi: 10.1021/bi00252a026.
We have examined proteins containing the DNA-binding domain of c-Myb with biophysical methods. This DNA-binding domain consists of three imperfect repeats (R1, R2, and R3) conserved among many species. Our results indicate that the DNA-binding domain forms unspecific and specific complexes with oligodeoxynucleotides. In the presence of R1, DNA sequences related to a canonical c-Myb-binding site are better discriminated. Furthermore, although R2 and R3 are sufficient for sequence-specific DNA binding, a structural change of the DNA-binding domain upon specific complex formation is induced only when R1 is present. Therefore, R1 might serve as an important element required for secondary structure alteration upon binding and its stabilization as well as for better discrimination between specific and related DNA sequences.
