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Bromodomain factor 1 (Bdf1) protein interacts with histones
Author(s) -
Pamblanco Mercè,
Poveda Ana,
Sendra Ramon,
Rodrı́guez-Navarro Susana,
Pérez-Ortı́n José E.,
Tordera Vicente
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02397-3
Subject(s) - bromodomain , histone h4 , histone , histone acetyltransferase , acetylation , amino acid , histone methyltransferase , chemistry , biochemistry , histone h3 , histone acetyltransferases , histone code , release factor , histone octamer , microbiology and biotechnology , biology , nucleosome , gene , ribosome , rna
Using a yeast two‐hybrid assay we detected an interaction between the N‐terminal region of histone H4 (amino acids 1–59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304–571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant 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.