The progress curves of the real-time biospecific interaction analysis based on surface plasmon resonance technology has been used to monitor the binding of the ETS1 oncoprotein basic domain to its specific DNA-binding site. The peptide corresponding to amino acids 364-K37N-400 of the human ETS1 oncoprotein was synthesized and used to test the hypothesis that this peptide contained sufficient information to bind DNA in a sequence- specific fashion. The 364-K37N-400 bound specifically and non- specifically (DNA lattice) to the ETS1 binding motif (CCGGAAGT) and bound non-specifically to the ETS1 binding motif containing the mutation (CCAGAAGT). The identification of the ERG-2 gene product using antibody raised against recombinant human ERG-2 protein has been shown. ERG-2 is a nuclear phosphoprotein and binds to purine-rich sequences (C/G)(C/a)GGAA(G/a)T.
