Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Genes, Reporter
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Histone Acetyltransferases
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Histones / metabolism*
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Protein Binding / physiology
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces
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Saccharomyces cerevisiae Proteins*
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Two-Hybrid System Techniques
Substances
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BDF1 protein, S cerevisiae
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Fungal Proteins
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Histones
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Peptide Fragments
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Acetyltransferases
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Histone Acetyltransferases