Abstract
We have developed a phage display technique for the mapping of protein-protein interaction sites and characterized the interaction between the c-myb proto-oncogene product and its co-activator CBP. Arbitrary DNA segments of the c-myb gene were cloned into a modified phagemid which allowed for expression in all possible reading frames. The mini-library 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 the CBP protein. Furthermore, an intramolecular interaction of the N-terminal Myb DNA binding domain with the C-terminus (amino acids 541–567) could be detected.