Using a yeast two-hybrid assay we detected an interaction between the N-ter
minal region of histone H4 (amino acids 1-59) and a fragment of the bromodo
main factor 1 protein (Bdf1p) (amino acids 304-571) that includes one of th
e two bromodomains of this protein, No interaction was observed using fragm
ents of histone H4 sequence smaller than the first 59 amino acids. Recombin
ant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but
not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and
H4 having different degrees of acetylation. Finally, we have not detected
histone acetyltransferase activity associated with Bdf1p, (C) 2001 Publishe
d by Elsevier Science B,V, on behalf of the Federation of European Biochemi
cal Societies.