Interaction of the Myb protein with specific DNA binding sites

Abstract

c-myb is expressed predominantly in proliferating immature hemopoietic cells and, like v-myb, functions as a transcriptional activator that displays sequence-specific DNA binding. Oncogenic activation of the c-myb protein (Myb) is associated with carboxyl-terminal and/or amino-terminal truncations, the former of which also potentiates Myb's transcriptional activation capacity. We show here that a carboxyl-truncated Myb protein binds with a 7-.fold higher affinity to an oligonucleotide bearing a Myb recognition sequence than does the full-length form. In addition, data are presented which show that Myb binds with different apparent affinities to variants of the recognition site and that Myb b..