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J Biol Chem, Vol. 274, Issue 20, 14422-14428, May 14, 1999
par,
áková,
k
Kozmik, andák
From the Institute of Molecular Genetics, Academy of Sciences of
the Czech Republic, Flemingovo 2, 166 37 Prague 6, Czech Republic
Using the yeast two-hybrid system, the
transcription factor ATBF1 was identified as v-Myb- and c-Myb-binding
protein. Deletion mutagenesis revealed amino acids 2484-2520 in human
ATBF1 and 279-300 in v-Myb as regions required for in
vitro binding of both proteins. Further experiments identified
leucines Leu325 and Leu332 of the Myb leucine
zipper motif as additional amino acid residues important for efficient
ATBF1-Myb interaction in vitro. In co-transfection experiments, the full-length ATBF1 was found to form in
vivo complexes with v-Myb and inhibit v-Myb transcriptional
activity. Both ATBF1 2484-2520 and Myb 279-300 regions were required
for the inhibitory effect. Finally, the chicken ATBF1 was identified,
showing high degree of amino acid sequence homology with human and
murine proteins. Our data reveal Myb proteins as the first ATBF1
partners detected so far and identify amino acids 279-300 in v-Myb as
a novel protein-protein interaction interface through which Myb
transcriptional activity can be regulated.
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