The nuclear oncogene v-myb and its cellular counterpart c-myb code for
proteins that bind to DNA in a sequence specific manner and act as re
gulators of transcription. The Myb protein contains DNA binding and tr
ansregulatory domains which are important for its function. The DNA bi
nding domain of Myb protein has been shown to contain three imperfectl
y conserved repeats of 50-52 aminoacids that constitute the amino term
inal end. In this communication, we show that Myb protein induces conf
ormational change in DNA after protein-DNA complex formation. Circular
permutation assays indicate that Myb protein induces DNA bending at t
he site of binding. Phasing analysis confirm the DNA bending and allow
ed the detection of relative orientation of bend. Myb proteins which c
omprise only DNA-binding domains either with three repeats or two repe
ats also bend DNA in the same orientation as the larger proteins with
both DNA-binding and transactivating domains. However, the transactiva
ting region seems to influence the magnitude of bend angle. We used mo
lecular modeling to analyse the structure of Myb-DNA complex formation
resulting in the bending of DNA. Data presented here show that Myb pr
otein, like other transcriptional regulators, bends DNA upon binding a
llowing the interaction of regulatory elements.