MAPPING OF PROTEIN-PROTEIN INTERACTIONS BETWEEN C-MYB AND ITS COACTIVATOR CBP BY A NEW PHAGE DISPLAY TECHNIQUE

We have developed a phage display technique for the mapping of protein -protein interaction sites and characterized the interaction between t he c-myb proto-oncogene product and its co-activator CBP. Arbitrary DN A segments of the c-myb gene were cloned into a modified phagemid whic h allowed for expression in all possible reading frames. The mini-libr ary encompassing all functional domains of the protein was propagated as phages and screened with different bait proteins. Alignment of the sequences revealed that the amino acids 317-342 of Myb interact with t he CBP protein. Furthermore, an intramolecular interaction of the N-te rminal Myb DNA binding domain with the C-terminus (amino acids 541-567 ) could be detected. (C) 1997 Federation of European Biochemical Socie ties.