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A direct link between core histone acetylation and transcriptionally active chromatin.
Author(s) -
Hebbes T. R.,
Thorne A. W.,
CraneRobinson C.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb02956.x
Subject(s) - biology , acetylation , histone , chromatin , histone code , microbiology and biotechnology , histone h1 , histone modifying enzymes , genetics , histone h2a , nucleosome , dna , gene
An antiserum raised against chemically acetylated histone H4 was found to recognize the epitope epsilon‐N‐acetyl lysine. Affinity‐purified antibodies were used to fractionate oligo‐ and mononucleosomal chromatin fragments from the nuclei of 15‐day chicken embryo erythrocytes. Antibody‐bound chromatin was found to contain elevated levels of acetylated core histones. On probing with sequences of alpha D globin, an actively transcribed gene, the antibody‐bound chromatin was 15‐ to 30‐fold enriched relative to the input chromatin. Using ovalbumin sequences as a probe, no enrichment was observed. The results demonstrate directly that transcriptionally active genes carry acetylated core histones.